In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure |
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Authors: | Loguercio Salvatore Dian Cyril Flagiello Angela Scannella Alessandra Pucci Piero Terradot Laurent Zagari Adriana |
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Institution: | Department of Biological Sciences and CNISM, University of Naples "Federico II", Via Mezzocannone 16, I-80134 Naples, Italy. |
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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. |
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