Differences between CusA and AcrB Crystallisation Highlighted by Protein Flexibility

被引：6

作者：

Deniaud, Aurelien

Goulielmakis, Aurelie

Coves, Jacques

Pebay-Peyroula, Eva

机构：

[1] Institut de Biologie Structurale Jean Pierre Ebel, UMR 5075 CEA-CNRS-Universite Joseph Fourier, Grenoble

来源：

PLOS ONE | 2009年 / 4卷 / 07期

关键词：

D O I：

10.1371/journal.pone.0006214

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

070301 [无机化学]; 070403 [天体物理学]; 070507 [自然资源与国土空间规划学]; 090105 [作物生产系统与生态工程];

摘要：

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.

引用

页数：9

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