The interdimeric interface controls function and stability of Ureaplasma urealiticum methionine S-adenosyltransferase
Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently e...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Kleiner, Daniel [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2019transfer abstract |
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| Schlagwörter: |
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| Umfang: |
21 |
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| Übergeordnetes Werk: |
Enthalten in: Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent - Wang, Yuntao ELSEVIER, 2015, JMB, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:431 ; year:2019 ; number:24 ; day:6 ; month:12 ; pages:4796-4816 ; extent:21 |
| Links: |
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| DOI / URN: |
10.1016/j.jmb.2019.09.003 |
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ELV048807907 |
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| 245 | 1 | 4 | |a The interdimeric interface controls function and stability of Ureaplasma urealiticum methionine S-adenosyltransferase |
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| 520 | |a Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. | ||
| 520 | |a Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. | ||
| 650 | 7 | |a X-ray crystallography |2 Elsevier | |
| 650 | 7 | |a Dihedral homotetramer |2 Elsevier | |
| 650 | 7 | |a Native-state MS |2 Elsevier | |
| 650 | 7 | |a Protein-protein interface evolution |2 Elsevier | |
| 650 | 7 | |a Methionine S-adenosyltransferase |2 Elsevier | |
| 700 | 1 | |a Shmulevich, Fannia |4 oth | |
| 700 | 1 | |a Zarivach, Raz |4 oth | |
| 700 | 1 | |a Shahar, Anat |4 oth | |
| 700 | 1 | |a Sharon, Michal |4 oth | |
| 700 | 1 | |a Ben-Nissan, Gili |4 oth | |
| 700 | 1 | |a Bershtein, Shimon |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a Wang, Yuntao ELSEVIER |t Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent |d 2015 |d JMB |g Amsterdam [u.a.] |w (DE-627)ELV012766127 |
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10.1016/j.jmb.2019.09.003 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000841.pica (DE-627)ELV048807907 (ELSEVIER)S0022-2836(19)30548-0 DE-627 ger DE-627 rakwb eng 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Kleiner, Daniel verfasserin aut The interdimeric interface controls function and stability of Ureaplasma urealiticum methionine S-adenosyltransferase 2019transfer abstract 21 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. X-ray crystallography Elsevier Dihedral homotetramer Elsevier Native-state MS Elsevier Protein-protein interface evolution Elsevier Methionine S-adenosyltransferase Elsevier Shmulevich, Fannia oth Zarivach, Raz oth Shahar, Anat oth Sharon, Michal oth Ben-Nissan, Gili oth Bershtein, Shimon oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:431 year:2019 number:24 day:6 month:12 pages:4796-4816 extent:21 https://doi.org/10.1016/j.jmb.2019.09.003 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 431 2019 24 6 1206 4796-4816 21 |
| spelling |
10.1016/j.jmb.2019.09.003 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000841.pica (DE-627)ELV048807907 (ELSEVIER)S0022-2836(19)30548-0 DE-627 ger DE-627 rakwb eng 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Kleiner, Daniel verfasserin aut The interdimeric interface controls function and stability of Ureaplasma urealiticum methionine S-adenosyltransferase 2019transfer abstract 21 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. X-ray crystallography Elsevier Dihedral homotetramer Elsevier Native-state MS Elsevier Protein-protein interface evolution Elsevier Methionine S-adenosyltransferase Elsevier Shmulevich, Fannia oth Zarivach, Raz oth Shahar, Anat oth Sharon, Michal oth Ben-Nissan, Gili oth Bershtein, Shimon oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:431 year:2019 number:24 day:6 month:12 pages:4796-4816 extent:21 https://doi.org/10.1016/j.jmb.2019.09.003 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 431 2019 24 6 1206 4796-4816 21 |
| allfields_unstemmed |
10.1016/j.jmb.2019.09.003 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000841.pica (DE-627)ELV048807907 (ELSEVIER)S0022-2836(19)30548-0 DE-627 ger DE-627 rakwb eng 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Kleiner, Daniel verfasserin aut The interdimeric interface controls function and stability of Ureaplasma urealiticum methionine S-adenosyltransferase 2019transfer abstract 21 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. X-ray crystallography Elsevier Dihedral homotetramer Elsevier Native-state MS Elsevier Protein-protein interface evolution Elsevier Methionine S-adenosyltransferase Elsevier Shmulevich, Fannia oth Zarivach, Raz oth Shahar, Anat oth Sharon, Michal oth Ben-Nissan, Gili oth Bershtein, Shimon oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:431 year:2019 number:24 day:6 month:12 pages:4796-4816 extent:21 https://doi.org/10.1016/j.jmb.2019.09.003 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 431 2019 24 6 1206 4796-4816 21 |
| allfieldsGer |
10.1016/j.jmb.2019.09.003 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000841.pica (DE-627)ELV048807907 (ELSEVIER)S0022-2836(19)30548-0 DE-627 ger DE-627 rakwb eng 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Kleiner, Daniel verfasserin aut The interdimeric interface controls function and stability of Ureaplasma urealiticum methionine S-adenosyltransferase 2019transfer abstract 21 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. X-ray crystallography Elsevier Dihedral homotetramer Elsevier Native-state MS Elsevier Protein-protein interface evolution Elsevier Methionine S-adenosyltransferase Elsevier Shmulevich, Fannia oth Zarivach, Raz oth Shahar, Anat oth Sharon, Michal oth Ben-Nissan, Gili oth Bershtein, Shimon oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:431 year:2019 number:24 day:6 month:12 pages:4796-4816 extent:21 https://doi.org/10.1016/j.jmb.2019.09.003 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 431 2019 24 6 1206 4796-4816 21 |
| allfieldsSound |
10.1016/j.jmb.2019.09.003 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000841.pica (DE-627)ELV048807907 (ELSEVIER)S0022-2836(19)30548-0 DE-627 ger DE-627 rakwb eng 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Kleiner, Daniel verfasserin aut The interdimeric interface controls function and stability of Ureaplasma urealiticum methionine S-adenosyltransferase 2019transfer abstract 21 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. X-ray crystallography Elsevier Dihedral homotetramer Elsevier Native-state MS Elsevier Protein-protein interface evolution Elsevier Methionine S-adenosyltransferase Elsevier Shmulevich, Fannia oth Zarivach, Raz oth Shahar, Anat oth Sharon, Michal oth Ben-Nissan, Gili oth Bershtein, Shimon oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:431 year:2019 number:24 day:6 month:12 pages:4796-4816 extent:21 https://doi.org/10.1016/j.jmb.2019.09.003 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 431 2019 24 6 1206 4796-4816 21 |
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English |
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Enthalten in Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent Amsterdam [u.a.] volume:431 year:2019 number:24 day:6 month:12 pages:4796-4816 extent:21 |
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Enthalten in Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent Amsterdam [u.a.] volume:431 year:2019 number:24 day:6 month:12 pages:4796-4816 extent:21 |
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X-ray crystallography Dihedral homotetramer Native-state MS Protein-protein interface evolution Methionine S-adenosyltransferase |
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Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent |
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Kleiner, Daniel @@aut@@ Shmulevich, Fannia @@oth@@ Zarivach, Raz @@oth@@ Shahar, Anat @@oth@@ Sharon, Michal @@oth@@ Ben-Nissan, Gili @@oth@@ Bershtein, Shimon @@oth@@ |
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interdimeric interface controls function and stability of ureaplasma urealiticum methionine s-adenosyltransferase |
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The interdimeric interface controls function and stability of Ureaplasma urealiticum methionine S-adenosyltransferase |
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Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. |
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Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. |
| abstract_unstemmed |
Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasma urealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a ∼45° shift in the dimer orientation and a concomitant ∼60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism. |
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The interdimeric interface controls function and stability of Ureaplasma urealiticum methionine S-adenosyltransferase |
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