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In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure.
Salvatore Loguercio
1 ,
Cyril Dian ,
Angela Flagiello ,
Alessandra Scannella ,
Piero Pucci ,
Laurent Terradot ,
Adriana Zagari
Oct 15 2008
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Abstract
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.