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
In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure / Loguercio, S., Dian, C., Flagiello, A., Scannella, A., Pucci, P., Terradot, L., Zagari, A.. - In: FEBS LETTERS. - ISSN 0014-5793. - STAMPA. - 582:23-24(2008), pp. 3537-3541. [10.1016/j.febslet.2008.09.025]
In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure
PUCCI, PIETRO;ZAGARI, ADRIANA
2008
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| File | Dimensione | Formato | |
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