The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli

Background ChaB is a putative regulator of ChaA, a $ Na^{+} $/$ H^{+} $ antiporter that also has $ Ca^{+} $/$ H^{+} $ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a struc...
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Autor*in:	Osborne, Michael J [verfasserIn] Siddiqui, Nadeem Iannuzzi, Pietro Gehring, Kalle

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2004

Schlagwörter:	NMR spectroscopy structure ChaA ChaB antiporter

Anmerkung:	© Osborne et al; licensee BioMed Central Ltd. 2004. This article is published under license to BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License (

Übergeordnetes Werk:	Enthalten in: BMC structural biology - London : BioMed Central, 2001, 4(2004), 1 vom: 11. Aug.
Übergeordnetes Werk:	volume:4 ; year:2004 ; number:1 ; day:11 ; month:08

Links:	Volltext

DOI / URN:	10.1186/1472-6807-4-9

Katalog-ID:	SPR028582780

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520			\|a Background ChaB is a putative regulator of ChaA, a $ Na^{+} $/$ H^{+} $ antiporter that also has $ Ca^{+} $/$ H^{+} $ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy. Results The structure of ChaB is composed of 3 α-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins. Conclusion ChaB is distinguished from its putative DNA binding sequence homologues by a highly charged flexible loop region that has weak affinity to $ Mg^{2+} $ and $ Ca^{2+} $ divalent metal ions.
650		4	\|a NMR spectroscopy \|7 (dpeaa)DE-He213
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650		4	\|a antiporter \|7 (dpeaa)DE-He213
700	1		\|a Siddiqui, Nadeem \|4 aut
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700	1		\|a Gehring, Kalle \|4 aut
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912			\|a GBV_USEFLAG_A
912			\|a SYSFLAG_A
912			\|a GBV_SPRINGER
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912			\|a GBV_ILN_20
912			\|a GBV_ILN_22
912			\|a GBV_ILN_23
912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_39
912			\|a GBV_ILN_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_95
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_151
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_206
912			\|a GBV_ILN_213
912			\|a GBV_ILN_230
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2008
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2031
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2057
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4367
912			\|a GBV_ILN_4700
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author_variant	m j o mj mjo n s ns p i pi k g kg
matchkey_str	article:14726807:2004----::hsltosrcuefhbpttvmmrninniotreua
hierarchy_sort_str	2004
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allfields	10.1186/1472-6807-4-9 doi (DE-627)SPR028582780 (SPR)1472-6807-4-9-e DE-627 ger DE-627 rakwb eng Osborne, Michael J verfasserin aut The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli 2004 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Osborne et al; licensee BioMed Central Ltd. 2004. This article is published under license to BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License ( Background ChaB is a putative regulator of ChaA, a $ Na^{+} $/$ H^{+} $ antiporter that also has $ Ca^{+} $/$ H^{+} $ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy. Results The structure of ChaB is composed of 3 α-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins. Conclusion ChaB is distinguished from its putative DNA binding sequence homologues by a highly charged flexible loop region that has weak affinity to $ Mg^{2+} $ and $ Ca^{2+} $ divalent metal ions. NMR spectroscopy (dpeaa)DE-He213 structure (dpeaa)DE-He213 ChaA (dpeaa)DE-He213 ChaB (dpeaa)DE-He213 antiporter (dpeaa)DE-He213 Siddiqui, Nadeem aut Iannuzzi, Pietro aut Gehring, Kalle aut Enthalten in BMC structural biology London : BioMed Central, 2001 4(2004), 1 vom: 11. Aug. (DE-627)331018810 (DE-600)2050440-8 1472-6807 nnns volume:4 year:2004 number:1 day:11 month:08 https://dx.doi.org/10.1186/1472-6807-4-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2004 1 11 08
spelling	10.1186/1472-6807-4-9 doi (DE-627)SPR028582780 (SPR)1472-6807-4-9-e DE-627 ger DE-627 rakwb eng Osborne, Michael J verfasserin aut The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli 2004 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Osborne et al; licensee BioMed Central Ltd. 2004. This article is published under license to BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License ( Background ChaB is a putative regulator of ChaA, a $ Na^{+} $/$ H^{+} $ antiporter that also has $ Ca^{+} $/$ H^{+} $ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy. Results The structure of ChaB is composed of 3 α-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins. Conclusion ChaB is distinguished from its putative DNA binding sequence homologues by a highly charged flexible loop region that has weak affinity to $ Mg^{2+} $ and $ Ca^{2+} $ divalent metal ions. NMR spectroscopy (dpeaa)DE-He213 structure (dpeaa)DE-He213 ChaA (dpeaa)DE-He213 ChaB (dpeaa)DE-He213 antiporter (dpeaa)DE-He213 Siddiqui, Nadeem aut Iannuzzi, Pietro aut Gehring, Kalle aut Enthalten in BMC structural biology London : BioMed Central, 2001 4(2004), 1 vom: 11. Aug. (DE-627)331018810 (DE-600)2050440-8 1472-6807 nnns volume:4 year:2004 number:1 day:11 month:08 https://dx.doi.org/10.1186/1472-6807-4-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2004 1 11 08
allfields_unstemmed	10.1186/1472-6807-4-9 doi (DE-627)SPR028582780 (SPR)1472-6807-4-9-e DE-627 ger DE-627 rakwb eng Osborne, Michael J verfasserin aut The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli 2004 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Osborne et al; licensee BioMed Central Ltd. 2004. This article is published under license to BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License ( Background ChaB is a putative regulator of ChaA, a $ Na^{+} $/$ H^{+} $ antiporter that also has $ Ca^{+} $/$ H^{+} $ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy. Results The structure of ChaB is composed of 3 α-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins. Conclusion ChaB is distinguished from its putative DNA binding sequence homologues by a highly charged flexible loop region that has weak affinity to $ Mg^{2+} $ and $ Ca^{2+} $ divalent metal ions. NMR spectroscopy (dpeaa)DE-He213 structure (dpeaa)DE-He213 ChaA (dpeaa)DE-He213 ChaB (dpeaa)DE-He213 antiporter (dpeaa)DE-He213 Siddiqui, Nadeem aut Iannuzzi, Pietro aut Gehring, Kalle aut Enthalten in BMC structural biology London : BioMed Central, 2001 4(2004), 1 vom: 11. Aug. (DE-627)331018810 (DE-600)2050440-8 1472-6807 nnns volume:4 year:2004 number:1 day:11 month:08 https://dx.doi.org/10.1186/1472-6807-4-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2004 1 11 08
allfieldsGer	10.1186/1472-6807-4-9 doi (DE-627)SPR028582780 (SPR)1472-6807-4-9-e DE-627 ger DE-627 rakwb eng Osborne, Michael J verfasserin aut The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli 2004 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Osborne et al; licensee BioMed Central Ltd. 2004. This article is published under license to BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License ( Background ChaB is a putative regulator of ChaA, a $ Na^{+} $/$ H^{+} $ antiporter that also has $ Ca^{+} $/$ H^{+} $ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy. Results The structure of ChaB is composed of 3 α-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins. Conclusion ChaB is distinguished from its putative DNA binding sequence homologues by a highly charged flexible loop region that has weak affinity to $ Mg^{2+} $ and $ Ca^{2+} $ divalent metal ions. NMR spectroscopy (dpeaa)DE-He213 structure (dpeaa)DE-He213 ChaA (dpeaa)DE-He213 ChaB (dpeaa)DE-He213 antiporter (dpeaa)DE-He213 Siddiqui, Nadeem aut Iannuzzi, Pietro aut Gehring, Kalle aut Enthalten in BMC structural biology London : BioMed Central, 2001 4(2004), 1 vom: 11. Aug. (DE-627)331018810 (DE-600)2050440-8 1472-6807 nnns volume:4 year:2004 number:1 day:11 month:08 https://dx.doi.org/10.1186/1472-6807-4-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2004 1 11 08
allfieldsSound	10.1186/1472-6807-4-9 doi (DE-627)SPR028582780 (SPR)1472-6807-4-9-e DE-627 ger DE-627 rakwb eng Osborne, Michael J verfasserin aut The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli 2004 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Osborne et al; licensee BioMed Central Ltd. 2004. This article is published under license to BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License ( Background ChaB is a putative regulator of ChaA, a $ Na^{+} $/$ H^{+} $ antiporter that also has $ Ca^{+} $/$ H^{+} $ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy. Results The structure of ChaB is composed of 3 α-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins. Conclusion ChaB is distinguished from its putative DNA binding sequence homologues by a highly charged flexible loop region that has weak affinity to $ Mg^{2+} $ and $ Ca^{2+} $ divalent metal ions. NMR spectroscopy (dpeaa)DE-He213 structure (dpeaa)DE-He213 ChaA (dpeaa)DE-He213 ChaB (dpeaa)DE-He213 antiporter (dpeaa)DE-He213 Siddiqui, Nadeem aut Iannuzzi, Pietro aut Gehring, Kalle aut Enthalten in BMC structural biology London : BioMed Central, 2001 4(2004), 1 vom: 11. Aug. (DE-627)331018810 (DE-600)2050440-8 1472-6807 nnns volume:4 year:2004 number:1 day:11 month:08 https://dx.doi.org/10.1186/1472-6807-4-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2004 1 11 08
language	English
source	Enthalten in BMC structural biology 4(2004), 1 vom: 11. Aug. volume:4 year:2004 number:1 day:11 month:08
sourceStr	Enthalten in BMC structural biology 4(2004), 1 vom: 11. Aug. volume:4 year:2004 number:1 day:11 month:08
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This article is published under license to BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License (</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Background ChaB is a putative regulator of ChaA, a $ Na^{+} $/$ H^{+} $ antiporter that also has $ Ca^{+} $/$ H^{+} $ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy. Results The structure of ChaB is composed of 3 α-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins. 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author	Osborne, Michael J
spellingShingle	Osborne, Michael J misc NMR spectroscopy misc structure misc ChaA misc ChaB misc antiporter The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli
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topic_title	The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli NMR spectroscopy (dpeaa)DE-He213 structure (dpeaa)DE-He213 ChaA (dpeaa)DE-He213 ChaB (dpeaa)DE-He213 antiporter (dpeaa)DE-He213
topic	misc NMR spectroscopy misc structure misc ChaA misc ChaB misc antiporter
topic_unstemmed	misc NMR spectroscopy misc structure misc ChaA misc ChaB misc antiporter
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title	The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli
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title_full	The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli
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author_browse	Osborne, Michael J Siddiqui, Nadeem Iannuzzi, Pietro Gehring, Kalle
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title_sort	solution structure of chab, a putative membrane ion antiporter regulator from escherichia coli
title_auth	The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli
abstract	Background ChaB is a putative regulator of ChaA, a $ Na^{+} $/$ H^{+} $ antiporter that also has $ Ca^{+} $/$ H^{+} $ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy. Results The structure of ChaB is composed of 3 α-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins. Conclusion ChaB is distinguished from its putative DNA binding sequence homologues by a highly charged flexible loop region that has weak affinity to $ Mg^{2+} $ and $ Ca^{2+} $ divalent metal ions. © Osborne et al; licensee BioMed Central Ltd. 2004. This article is published under license to BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License (
abstractGer	Background ChaB is a putative regulator of ChaA, a $ Na^{+} $/$ H^{+} $ antiporter that also has $ Ca^{+} $/$ H^{+} $ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy. Results The structure of ChaB is composed of 3 α-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins. Conclusion ChaB is distinguished from its putative DNA binding sequence homologues by a highly charged flexible loop region that has weak affinity to $ Mg^{2+} $ and $ Ca^{2+} $ divalent metal ions. © Osborne et al; licensee BioMed Central Ltd. 2004. This article is published under license to BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License (
abstract_unstemmed	Background ChaB is a putative regulator of ChaA, a $ Na^{+} $/$ H^{+} $ antiporter that also has $ Ca^{+} $/$ H^{+} $ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy. Results The structure of ChaB is composed of 3 α-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins. Conclusion ChaB is distinguished from its putative DNA binding sequence homologues by a highly charged flexible loop region that has weak affinity to $ Mg^{2+} $ and $ Ca^{2+} $ divalent metal ions. © Osborne et al; licensee BioMed Central Ltd. 2004. This article is published under license to BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License (
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title_short	The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli
url	https://dx.doi.org/10.1186/1472-6807-4-9
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author2	Siddiqui, Nadeem Iannuzzi, Pietro Gehring, Kalle
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up_date	2024-07-03T20:22:15.397Z
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This article is published under license to BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License (</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Background ChaB is a putative regulator of ChaA, a $ Na^{+} $/$ H^{+} $ antiporter that also has $ Ca^{+} $/$ H^{+} $ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy. Results The structure of ChaB is composed of 3 α-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins. Conclusion ChaB is distinguished from its putative DNA binding sequence homologues by a highly charged flexible loop region that has weak affinity to $ Mg^{2+} $ and $ Ca^{2+} $ divalent metal ions.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">NMR spectroscopy</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">structure</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">ChaA</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">ChaB</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">antiporter</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Siddiqui, Nadeem</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Iannuzzi, Pietro</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gehring, Kalle</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">BMC structural biology</subfield><subfield code="d">London : BioMed Central, 2001</subfield><subfield code="g">4(2004), 1 vom: 11. 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The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli

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