http://www.cnr.it/ontology/cnr/individuo/prodotto/ID13872
In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure (Articolo in rivista)
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- In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure (Articolo in rivista) (literal)
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- 2008-01-01T00:00:00+01:00 (literal)
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Loguercio S, Dian C, Flagiello A, Scannella A, Pucci P, Terradot L, Zagari A (2008)
In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure
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- Loguercio S, Dian C, Flagiello A, Scannella A, Pucci P, Terradot L, Zagari A (literal)
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- a Department of Biological Sciences and CNISM, University of Naples ''Federico II'', Via Mezzocannone 16, I-80134 Naples, Italy
b European Synchrotron Radiation Facility, BP 220 F-38043, Grenoble Cedex 9, France
c CEINGE - Biotecnologie Avanzate Scarl, Naples, Italy
d Department of Organic Chemistry and Biochemistry, University of Naples ''Federico II'', Naples, Italy
e IBB istituto di Biostrutture e bioimmagini- CNR (literal)
- Titolo
- In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure (literal)
- 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. (literal)
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