In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure

Salvatore Loguercio; Cyril Dian; Angela Flagiello; Alessandra Scannella; Piero Pucci; Laurent Terradot; Adriana Zagari

doi:10.1016/j.febslet.2008.09.025

In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure

FEBS Lett. 2008 Oct 15;582(23-24):3537-41. doi: 10.1016/j.febslet.2008.09.025. Epub 2008 Sep 19.

Authors

Salvatore Loguercio¹, Cyril Dian, Angela Flagiello, Alessandra Scannella, Piero Pucci, Laurent Terradot, Adriana Zagari

Affiliation

¹ Department of Biological Sciences and CNISM, University of Naples "Federico II", Via Mezzocannone 16, I-80134 Naples, Italy.

PMID: 18805417
DOI: 10.1016/j.febslet.2008.09.025

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Amino Acid Substitution
Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Cysteine / chemistry*
Cysteine / genetics
Heat-Shock Proteins / chemistry*
Heat-Shock Proteins / genetics
Helicobacter pylori / metabolism*
Models, Molecular
Molecular Sequence Data
Mutation
Protein Structure, Tertiary

Substances

Bacterial Proteins
Heat-Shock Proteins
HspA protein, bacteria
Cysteine