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 structural genomics proj...

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Detalles Bibliográficos
Autores principales: Osborne, Michael J, Siddiqui, Nadeem, Iannuzzi, Pietro, Gehring, Kalle
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2004
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC514712/
https://www.ncbi.nlm.nih.gov/pubmed/15306028
http://dx.doi.org/10.1186/1472-6807-4-9
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author Osborne, Michael J
Siddiqui, Nadeem
Iannuzzi, Pietro
Gehring, Kalle
author_facet Osborne, Michael J
Siddiqui, Nadeem
Iannuzzi, Pietro
Gehring, Kalle
author_sort Osborne, Michael J
collection PubMed
description 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.
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spelling pubmed-5147122004-08-29 The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli Osborne, Michael J Siddiqui, Nadeem Iannuzzi, Pietro Gehring, Kalle BMC Struct Biol Research Article 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. BioMed Central 2004-08-11 /pmc/articles/PMC514712/ /pubmed/15306028 http://dx.doi.org/10.1186/1472-6807-4-9 Text en Copyright © 2004 Osborne et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open-access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Osborne, Michael J
Siddiqui, Nadeem
Iannuzzi, Pietro
Gehring, Kalle
The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli
title The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli
title_full The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli
title_fullStr The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli
title_full_unstemmed The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli
title_short The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli
title_sort solution structure of chab, a putative membrane ion antiporter regulator from escherichia coli
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC514712/
https://www.ncbi.nlm.nih.gov/pubmed/15306028
http://dx.doi.org/10.1186/1472-6807-4-9
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