Document Detail


The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold.
MedLine Citation:
PMID:  15081815     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The terminal branch of the general secretion pathway (Gsp or type II secretion system) is used by several pathogenic bacteria for the secretion of their virulence factors across the outer membrane. In these secretion systems, a complex of 12-15 Gsp proteins spans from the pore in the outer membrane via several associated signal or energy-transducing proteins in the inner membrane to a regulating ATPase in the cytosol. The human pathogen Vibrio cholerae uses such a system, called the Eps system, for the export of the cholera toxin and other virulence factors from its periplasm into the lumen of the gastrointestinal tract of the host. Here, we report the atomic structure of the periplasmic domain of the EpsM protein from V.cholerae, which is a part of the interface between the regulating part and the rest of the Eps system. The crystal structure was determined by Se-Met MAD phasing and the model was refined to 1.7A resolution. The monomer consists of two alphabetabeta-subdomains forming a sandwich of two alpha-helices and a four-stranded antiparallel beta-sheet. In the dimer, a deep cleft with a polar rim and a hydrophobic bottom made by conserved residues is located between the monomers. This cleft contains an extra electron density suggesting that this region might serve as a binding site of an unknown ligand or part of a protein partner. Unexpectedly, the fold of the periplasmic domain of EpsM is an undescribed circular permutation of the ferredoxin fold.
Authors:
Jan Abendroth; Adrian E Rice; Karen McLuskey; Michael Bagdasarian; Wim G J Hol
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Journal of molecular biology     Volume:  338     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2004 Apr 
Date Detail:
Created Date:  2004-04-14     Completed Date:  2004-05-19     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  585-96     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Biomolecular Structure Center, School of Medicine, University of Washington, Box 357742, Seattle, WA 98195-7242, USA.
Data Bank Information
Bank Name/Acc. No.:
PDB/1UV7
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / chemistry*,  genetics
Chromatography, Gel
Conserved Sequence
Membrane Proteins / chemistry*,  genetics
Molecular Sequence Data
Multigene Family
Protein Structure, Quaternary
Protein Structure, Tertiary
Sequence Alignment
Vibrio cholerae / chemistry*,  genetics
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/EpsM protein, Vibrio cholerae; 0/Membrane Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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