In HspA from  Helicobacter pylori  vicinal disulfide bridges are a key determinant of domain B structure | Zendy

Loguercio Salvatore | Zendy; Dian Cyril | Zendy; Flagiello Angela | Zendy; Scannella Alessandra | Zendy; Pucci Piero | Zendy; Terradot Laurent | Zendy; Zagari Adriana | Zendy

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In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure

Author(s) -

Loguercio Salvatore,

Dian Cyril,

Flagiello Angela,

Scannella Alessandra,

Pucci Piero,

Terradot Laurent,

Zagari Adriana

Publication year - 2008

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2008.09.025

Subject(s) - egf like domain , helicobacter pylori , chemistry , mutant , disulfide bond , domain (mathematical analysis) , heat shock protein , protein disulfide isomerase , stereochemistry , biochemistry , microbiology and biotechnology , biology , binding domain , binding site , genetics , mathematical analysis , mathematics , gene

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.

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