Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes
Anthrax toxin is an intracellularly acting toxin in which sufficient information is available regarding the structure of its transmembrane channel, allowing for detailed investigation of models of translocation. Anthrax toxin, comprising three proteins-protective antigen (PA), lethal factor (LF), an...
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| Autor*in: |
Das, Debasis [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016 |
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| Rechteinformationen: |
Nutzungsrecht: © COPYRIGHT 2016 National Academy of Sciences |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Proceedings of the National Academy of Sciences of the United States of America - Washington, DC : NAS, 1877, 113(2016), 34, Seite 9611-9616 |
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| Übergeordnetes Werk: |
volume:113 ; year:2016 ; number:34 ; pages:9611-9616 |
| Links: |
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| DOI / URN: |
10.1073/pnas.1600624113 |
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| 245 | 1 | 0 | |a Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes |
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| 520 | |a Anthrax toxin is an intracellularly acting toxin in which sufficient information is available regarding the structure of its transmembrane channel, allowing for detailed investigation of models of translocation. Anthrax toxin, comprising three proteins-protective antigen (PA), lethal factor (LF), and edema factor-translocates large proteins across membranes. Here we show that the PA translocase channel has a transport function in which its catalytic active sites operate allosterically. We find that the phenylalanine clamp (ϕ-clamp), the known conductance bottleneck in the PA translocase, gates as either a more closed state or a more dilated state. Thermodynamically, the two channel states have >300-fold different binding affinities for an LF-derived peptide. The change in clamp thermodynamics requires distant α-clamp and ϕ-clamp sites. Clamp allostery and translocation are more optimal for LF peptides with uniform stereochemistry, where the least allosteric and least efficiently translocated peptide had a mixed stereochemistry. Overall, the kinetic results are in less agreement with an extended-chain Brownian ratchet model but, instead, are more consistent with an allosteric helix-compression model that is dependent also on substrate peptide coil-to-helix/helix-to-coil cooperativity. | ||
| 540 | |a Nutzungsrecht: © COPYRIGHT 2016 National Academy of Sciences | ||
| 650 | 4 | |a Translocation (Genetics) | |
| 650 | 4 | |a Health aspects | |
| 650 | 4 | |a Methods | |
| 650 | 4 | |a Allometry | |
| 650 | 4 | |a Anthrax | |
| 650 | 4 | |a Peptides | |
| 650 | 4 | |a Genetic aspects | |
| 650 | 4 | |a Proteins | |
| 650 | 4 | |a Antigens | |
| 650 | 4 | |a Thermodynamics | |
| 700 | 1 | |a Krantz, Bryan A |4 oth | |
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10.1073/pnas.1600624113 doi PQ20161012 (DE-627)OLC1983744565 (DE-599)GBVOLC1983744565 (PRQ)c1381-cf68775687b7377c9391531aa56e16f67e63201444a0cf3c93b73a6c3328bda50 (KEY)0583363920160000113003409611peptideandprotondrivenallostericclampscatalyzeanth DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Das, Debasis verfasserin aut Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Anthrax toxin is an intracellularly acting toxin in which sufficient information is available regarding the structure of its transmembrane channel, allowing for detailed investigation of models of translocation. Anthrax toxin, comprising three proteins-protective antigen (PA), lethal factor (LF), and edema factor-translocates large proteins across membranes. Here we show that the PA translocase channel has a transport function in which its catalytic active sites operate allosterically. We find that the phenylalanine clamp (ϕ-clamp), the known conductance bottleneck in the PA translocase, gates as either a more closed state or a more dilated state. Thermodynamically, the two channel states have >300-fold different binding affinities for an LF-derived peptide. The change in clamp thermodynamics requires distant α-clamp and ϕ-clamp sites. Clamp allostery and translocation are more optimal for LF peptides with uniform stereochemistry, where the least allosteric and least efficiently translocated peptide had a mixed stereochemistry. Overall, the kinetic results are in less agreement with an extended-chain Brownian ratchet model but, instead, are more consistent with an allosteric helix-compression model that is dependent also on substrate peptide coil-to-helix/helix-to-coil cooperativity. Nutzungsrecht: © COPYRIGHT 2016 National Academy of Sciences Translocation (Genetics) Health aspects Methods Allometry Anthrax Peptides Genetic aspects Proteins Antigens Thermodynamics Krantz, Bryan A oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 113(2016), 34, Seite 9611-9616 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:113 year:2016 number:34 pages:9611-9616 http://dx.doi.org/10.1073/pnas.1600624113 Volltext http://www.ncbi.nlm.nih.gov/pubmed/27506790 http://search.proquest.com/docview/1819111942 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 113 2016 34 9611-9616 |
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10.1073/pnas.1600624113 doi PQ20161012 (DE-627)OLC1983744565 (DE-599)GBVOLC1983744565 (PRQ)c1381-cf68775687b7377c9391531aa56e16f67e63201444a0cf3c93b73a6c3328bda50 (KEY)0583363920160000113003409611peptideandprotondrivenallostericclampscatalyzeanth DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Das, Debasis verfasserin aut Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Anthrax toxin is an intracellularly acting toxin in which sufficient information is available regarding the structure of its transmembrane channel, allowing for detailed investigation of models of translocation. Anthrax toxin, comprising three proteins-protective antigen (PA), lethal factor (LF), and edema factor-translocates large proteins across membranes. Here we show that the PA translocase channel has a transport function in which its catalytic active sites operate allosterically. We find that the phenylalanine clamp (ϕ-clamp), the known conductance bottleneck in the PA translocase, gates as either a more closed state or a more dilated state. Thermodynamically, the two channel states have >300-fold different binding affinities for an LF-derived peptide. The change in clamp thermodynamics requires distant α-clamp and ϕ-clamp sites. Clamp allostery and translocation are more optimal for LF peptides with uniform stereochemistry, where the least allosteric and least efficiently translocated peptide had a mixed stereochemistry. Overall, the kinetic results are in less agreement with an extended-chain Brownian ratchet model but, instead, are more consistent with an allosteric helix-compression model that is dependent also on substrate peptide coil-to-helix/helix-to-coil cooperativity. Nutzungsrecht: © COPYRIGHT 2016 National Academy of Sciences Translocation (Genetics) Health aspects Methods Allometry Anthrax Peptides Genetic aspects Proteins Antigens Thermodynamics Krantz, Bryan A oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 113(2016), 34, Seite 9611-9616 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:113 year:2016 number:34 pages:9611-9616 http://dx.doi.org/10.1073/pnas.1600624113 Volltext http://www.ncbi.nlm.nih.gov/pubmed/27506790 http://search.proquest.com/docview/1819111942 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 113 2016 34 9611-9616 |
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10.1073/pnas.1600624113 doi PQ20161012 (DE-627)OLC1983744565 (DE-599)GBVOLC1983744565 (PRQ)c1381-cf68775687b7377c9391531aa56e16f67e63201444a0cf3c93b73a6c3328bda50 (KEY)0583363920160000113003409611peptideandprotondrivenallostericclampscatalyzeanth DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Das, Debasis verfasserin aut Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Anthrax toxin is an intracellularly acting toxin in which sufficient information is available regarding the structure of its transmembrane channel, allowing for detailed investigation of models of translocation. Anthrax toxin, comprising three proteins-protective antigen (PA), lethal factor (LF), and edema factor-translocates large proteins across membranes. Here we show that the PA translocase channel has a transport function in which its catalytic active sites operate allosterically. We find that the phenylalanine clamp (ϕ-clamp), the known conductance bottleneck in the PA translocase, gates as either a more closed state or a more dilated state. Thermodynamically, the two channel states have >300-fold different binding affinities for an LF-derived peptide. The change in clamp thermodynamics requires distant α-clamp and ϕ-clamp sites. Clamp allostery and translocation are more optimal for LF peptides with uniform stereochemistry, where the least allosteric and least efficiently translocated peptide had a mixed stereochemistry. Overall, the kinetic results are in less agreement with an extended-chain Brownian ratchet model but, instead, are more consistent with an allosteric helix-compression model that is dependent also on substrate peptide coil-to-helix/helix-to-coil cooperativity. Nutzungsrecht: © COPYRIGHT 2016 National Academy of Sciences Translocation (Genetics) Health aspects Methods Allometry Anthrax Peptides Genetic aspects Proteins Antigens Thermodynamics Krantz, Bryan A oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 113(2016), 34, Seite 9611-9616 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:113 year:2016 number:34 pages:9611-9616 http://dx.doi.org/10.1073/pnas.1600624113 Volltext http://www.ncbi.nlm.nih.gov/pubmed/27506790 http://search.proquest.com/docview/1819111942 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 113 2016 34 9611-9616 |
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10.1073/pnas.1600624113 doi PQ20161012 (DE-627)OLC1983744565 (DE-599)GBVOLC1983744565 (PRQ)c1381-cf68775687b7377c9391531aa56e16f67e63201444a0cf3c93b73a6c3328bda50 (KEY)0583363920160000113003409611peptideandprotondrivenallostericclampscatalyzeanth DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Das, Debasis verfasserin aut Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Anthrax toxin is an intracellularly acting toxin in which sufficient information is available regarding the structure of its transmembrane channel, allowing for detailed investigation of models of translocation. Anthrax toxin, comprising three proteins-protective antigen (PA), lethal factor (LF), and edema factor-translocates large proteins across membranes. Here we show that the PA translocase channel has a transport function in which its catalytic active sites operate allosterically. We find that the phenylalanine clamp (ϕ-clamp), the known conductance bottleneck in the PA translocase, gates as either a more closed state or a more dilated state. Thermodynamically, the two channel states have >300-fold different binding affinities for an LF-derived peptide. The change in clamp thermodynamics requires distant α-clamp and ϕ-clamp sites. Clamp allostery and translocation are more optimal for LF peptides with uniform stereochemistry, where the least allosteric and least efficiently translocated peptide had a mixed stereochemistry. Overall, the kinetic results are in less agreement with an extended-chain Brownian ratchet model but, instead, are more consistent with an allosteric helix-compression model that is dependent also on substrate peptide coil-to-helix/helix-to-coil cooperativity. Nutzungsrecht: © COPYRIGHT 2016 National Academy of Sciences Translocation (Genetics) Health aspects Methods Allometry Anthrax Peptides Genetic aspects Proteins Antigens Thermodynamics Krantz, Bryan A oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 113(2016), 34, Seite 9611-9616 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:113 year:2016 number:34 pages:9611-9616 http://dx.doi.org/10.1073/pnas.1600624113 Volltext http://www.ncbi.nlm.nih.gov/pubmed/27506790 http://search.proquest.com/docview/1819111942 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 113 2016 34 9611-9616 |
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10.1073/pnas.1600624113 doi PQ20161012 (DE-627)OLC1983744565 (DE-599)GBVOLC1983744565 (PRQ)c1381-cf68775687b7377c9391531aa56e16f67e63201444a0cf3c93b73a6c3328bda50 (KEY)0583363920160000113003409611peptideandprotondrivenallostericclampscatalyzeanth DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Das, Debasis verfasserin aut Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Anthrax toxin is an intracellularly acting toxin in which sufficient information is available regarding the structure of its transmembrane channel, allowing for detailed investigation of models of translocation. Anthrax toxin, comprising three proteins-protective antigen (PA), lethal factor (LF), and edema factor-translocates large proteins across membranes. Here we show that the PA translocase channel has a transport function in which its catalytic active sites operate allosterically. We find that the phenylalanine clamp (ϕ-clamp), the known conductance bottleneck in the PA translocase, gates as either a more closed state or a more dilated state. Thermodynamically, the two channel states have >300-fold different binding affinities for an LF-derived peptide. The change in clamp thermodynamics requires distant α-clamp and ϕ-clamp sites. Clamp allostery and translocation are more optimal for LF peptides with uniform stereochemistry, where the least allosteric and least efficiently translocated peptide had a mixed stereochemistry. Overall, the kinetic results are in less agreement with an extended-chain Brownian ratchet model but, instead, are more consistent with an allosteric helix-compression model that is dependent also on substrate peptide coil-to-helix/helix-to-coil cooperativity. Nutzungsrecht: © COPYRIGHT 2016 National Academy of Sciences Translocation (Genetics) Health aspects Methods Allometry Anthrax Peptides Genetic aspects Proteins Antigens Thermodynamics Krantz, Bryan A oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 113(2016), 34, Seite 9611-9616 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:113 year:2016 number:34 pages:9611-9616 http://dx.doi.org/10.1073/pnas.1600624113 Volltext http://www.ncbi.nlm.nih.gov/pubmed/27506790 http://search.proquest.com/docview/1819111942 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 113 2016 34 9611-9616 |
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peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes |
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Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes |
| abstract |
Anthrax toxin is an intracellularly acting toxin in which sufficient information is available regarding the structure of its transmembrane channel, allowing for detailed investigation of models of translocation. Anthrax toxin, comprising three proteins-protective antigen (PA), lethal factor (LF), and edema factor-translocates large proteins across membranes. Here we show that the PA translocase channel has a transport function in which its catalytic active sites operate allosterically. We find that the phenylalanine clamp (ϕ-clamp), the known conductance bottleneck in the PA translocase, gates as either a more closed state or a more dilated state. Thermodynamically, the two channel states have >300-fold different binding affinities for an LF-derived peptide. The change in clamp thermodynamics requires distant α-clamp and ϕ-clamp sites. Clamp allostery and translocation are more optimal for LF peptides with uniform stereochemistry, where the least allosteric and least efficiently translocated peptide had a mixed stereochemistry. Overall, the kinetic results are in less agreement with an extended-chain Brownian ratchet model but, instead, are more consistent with an allosteric helix-compression model that is dependent also on substrate peptide coil-to-helix/helix-to-coil cooperativity. |
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Anthrax toxin is an intracellularly acting toxin in which sufficient information is available regarding the structure of its transmembrane channel, allowing for detailed investigation of models of translocation. Anthrax toxin, comprising three proteins-protective antigen (PA), lethal factor (LF), and edema factor-translocates large proteins across membranes. Here we show that the PA translocase channel has a transport function in which its catalytic active sites operate allosterically. We find that the phenylalanine clamp (ϕ-clamp), the known conductance bottleneck in the PA translocase, gates as either a more closed state or a more dilated state. Thermodynamically, the two channel states have >300-fold different binding affinities for an LF-derived peptide. The change in clamp thermodynamics requires distant α-clamp and ϕ-clamp sites. Clamp allostery and translocation are more optimal for LF peptides with uniform stereochemistry, where the least allosteric and least efficiently translocated peptide had a mixed stereochemistry. Overall, the kinetic results are in less agreement with an extended-chain Brownian ratchet model but, instead, are more consistent with an allosteric helix-compression model that is dependent also on substrate peptide coil-to-helix/helix-to-coil cooperativity. |
| abstract_unstemmed |
Anthrax toxin is an intracellularly acting toxin in which sufficient information is available regarding the structure of its transmembrane channel, allowing for detailed investigation of models of translocation. Anthrax toxin, comprising three proteins-protective antigen (PA), lethal factor (LF), and edema factor-translocates large proteins across membranes. Here we show that the PA translocase channel has a transport function in which its catalytic active sites operate allosterically. We find that the phenylalanine clamp (ϕ-clamp), the known conductance bottleneck in the PA translocase, gates as either a more closed state or a more dilated state. Thermodynamically, the two channel states have >300-fold different binding affinities for an LF-derived peptide. The change in clamp thermodynamics requires distant α-clamp and ϕ-clamp sites. Clamp allostery and translocation are more optimal for LF peptides with uniform stereochemistry, where the least allosteric and least efficiently translocated peptide had a mixed stereochemistry. Overall, the kinetic results are in less agreement with an extended-chain Brownian ratchet model but, instead, are more consistent with an allosteric helix-compression model that is dependent also on substrate peptide coil-to-helix/helix-to-coil cooperativity. |
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Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes |
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