In HspA from Helicobacter pylori

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• 作者：Salvatore Loguercio ; Cyril Dian ; Angela Flagiello ; Aless ; ra Scannella ; Piero Pucci ; Laurent Terradot ; Adriana Zagari
• 关键词：Small heat shock protein ; Chaperonin GroES ; Nickel binding protein ; Mass spectrometry ; Helicobacter pylori
• 刊名：FEBS Letters
• 出版年：2008
• 出版时间：15 October 2008
• 年：2008
• 卷：582
• 期：23-24
• 页码：3537-3541
• 全文大小：623 K

文摘

Helicobacter pylori produces a heat shock protein A (HspA) that is unique to this bacteria. While the first 91 residues (domain A) of the protein are similar to GroES, the last 26 (domain B) are unique to HspA. Domain B contains eight histidines and four cysteines and was suggested to bind nickel. We have produced HspA and two mutants: Cys94Ala and Cys94Ala/Cys111Ala and identified the disulfide bridge pattern of the protein. We found that the cysteines are engaged in three disulfide bonds: Cys51/Cys53, Cys94/Cys111 and Cys95/Cys112 that result in a unique closed loop structure for the domain B.