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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.