Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8384144 | FEBS Letters | 2008 | 5 Pages |
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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Authors
Salvatore Loguercio, Cyril Dian, Angela Flagiello, Alessandra Scannella, Piero Pucci, Laurent Terradot, Adriana Zagari,