Document Detail

Helicobacter pylori acidic stress response factor HP1286 is a YceI homolog with new binding specificity.
MedLine Citation:
PMID:  20236316     Owner:  NLM     Status:  MEDLINE    
HP1286 from Helicobacter pylori is among the proteins that play a relevant role in bacterial colonization and persistence in the stomach. Indeed, it was demonstrated to be overexpressed under acidic stress conditions, together with other essential virulence factors. Here we describe its crystal structure, determined at 2.1 A resolution. The molecular model, a dimer characterized by two-fold symmetry, shows that HP1286 structurally belongs to the YceI-like protein family, which in turn is characterized by the lipocalin fold. The latter characterizes proteins possessing an internal cavity with the function of binding and/or transport of amphiphilic molecules. Surprisingly, a molecule of erucamide was found bound in the internal cavity of each monomer of recombinant HP1286, cloned and expressed in an Escherichia coli heterologous system. The shape and length of the cavity indicate that, at variance with other members of the family, HP-YceI has a binding specificity for amphiphilic compounds with a linear chain of about 22 carbon atoms. These features, along with the fact that the protein is secreted by the bacterium and is involved in adaptation to an acidic environment, suggest that its function could be that of sequestering specific fatty acids or amides from the environment, either to supply the bacterium with the fatty acids necessary for its metabolism, or to protect and detoxify it from the detergent-like antimicrobial activity of fatty acids that are eventually present in the external milieu.
Lorenza Sisinni; Laura Cendron; Gabriella Favaro; Giuseppe Zanotti
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-03-03
Journal Detail:
Title:  The FEBS journal     Volume:  277     ISSN:  1742-4658     ISO Abbreviation:  FEBS J.     Publication Date:  2010 Apr 
Date Detail:
Created Date:  2010-04-16     Completed Date:  2010-05-12     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  England    
Other Details:
Languages:  eng     Pagination:  1896-905     Citation Subset:  IM    
Department of Biological Chemistry, University of Padua, Padua, Italy.
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MeSH Terms
Acids / metabolism*
Amino Acid Sequence
Bacterial Proteins / chemistry,  genetics,  metabolism
Binding Sites / genetics
Cloning, Molecular
Erucic Acids / metabolism
Escherichia coli / genetics
Heat-Shock Proteins / genetics,  isolation & purification,  metabolism*
Helicobacter pylori / metabolism*
Hydrogen Bonding
Models, Molecular
Molecular Sequence Data
Protein Binding / genetics
Protein Conformation
Protein Structure, Secondary
Recombinant Proteins / chemistry,  metabolism
Sequence Homology, Amino Acid
Reg. No./Substance:
0/Acids; 0/Bacterial Proteins; 0/Erucic Acids; 0/Heat-Shock Proteins; 0/Recombinant Proteins; 112-84-5/erucyl amide

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