Differences between CusA and AcrB Crystallisation Highlighted by Protein Flexibility

BACKGROUND: Until very recently, AcrB was the only Resistance Nodulation and cell Division transporter for which the structure has been elucidated. Towards a general understanding of this protein family, CusA and AcrB were compared. METHODOLOGY/PRINCIPAL FINDINGS: In dodecylmaltoside, AcrB crystalli...

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Autores principales: Deniaud, Aurélien, Goulielmakis, Aurélie, Covès, Jacques, Pebay-Peyroula, Eva
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2009
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2704858/
https://www.ncbi.nlm.nih.gov/pubmed/19593437
http://dx.doi.org/10.1371/journal.pone.0006214
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author Deniaud, Aurélien
Goulielmakis, Aurélie
Covès, Jacques
Pebay-Peyroula, Eva
author_facet Deniaud, Aurélien
Goulielmakis, Aurélie
Covès, Jacques
Pebay-Peyroula, Eva
author_sort Deniaud, Aurélien
collection PubMed
description BACKGROUND: Until very recently, AcrB was the only Resistance Nodulation and cell Division transporter for which the structure has been elucidated. Towards a general understanding of this protein family, CusA and AcrB were compared. METHODOLOGY/PRINCIPAL FINDINGS: In dodecylmaltoside, AcrB crystallised in many different conditions, while CusA does not. This could be due to the difference in dynamic between these proteins as judged from limited proteolysis assays. Addition of various compounds, in particular heavy metal cations, stabilises CusA. CONCLUSION/SIGNIFICANCE: This approach could constitute a first step towards CusA crystallisation.
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spelling pubmed-27048582009-07-10 Differences between CusA and AcrB Crystallisation Highlighted by Protein Flexibility Deniaud, Aurélien Goulielmakis, Aurélie Covès, Jacques Pebay-Peyroula, Eva PLoS One Research Article BACKGROUND: Until very recently, AcrB was the only Resistance Nodulation and cell Division transporter for which the structure has been elucidated. Towards a general understanding of this protein family, CusA and AcrB were compared. METHODOLOGY/PRINCIPAL FINDINGS: In dodecylmaltoside, AcrB crystallised in many different conditions, while CusA does not. This could be due to the difference in dynamic between these proteins as judged from limited proteolysis assays. Addition of various compounds, in particular heavy metal cations, stabilises CusA. CONCLUSION/SIGNIFICANCE: This approach could constitute a first step towards CusA crystallisation. Public Library of Science 2009-07-10 /pmc/articles/PMC2704858/ /pubmed/19593437 http://dx.doi.org/10.1371/journal.pone.0006214 Text en Deniaud et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Deniaud, Aurélien
Goulielmakis, Aurélie
Covès, Jacques
Pebay-Peyroula, Eva
Differences between CusA and AcrB Crystallisation Highlighted by Protein Flexibility
title Differences between CusA and AcrB Crystallisation Highlighted by Protein Flexibility
title_full Differences between CusA and AcrB Crystallisation Highlighted by Protein Flexibility
title_fullStr Differences between CusA and AcrB Crystallisation Highlighted by Protein Flexibility
title_full_unstemmed Differences between CusA and AcrB Crystallisation Highlighted by Protein Flexibility
title_short Differences between CusA and AcrB Crystallisation Highlighted by Protein Flexibility
title_sort differences between cusa and acrb crystallisation highlighted by protein flexibility
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2704858/
https://www.ncbi.nlm.nih.gov/pubmed/19593437
http://dx.doi.org/10.1371/journal.pone.0006214
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