Document Detail


NanC crystal structure, a model for outer-membrane channels of the acidic sugar-specific KdgM porin family.
MedLine Citation:
PMID:  19796645     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Sialic acids are acidic sugars present mostly on vertebrate cell surfaces, which can be metabolized by bacteria and act as an inflammation signal. N-Acetylneuraminic acid, the most abundant sialic acid, can enter into Escherichia coli K12 through NanC, an N-acetylneuraminic acid-inducible outer-membrane channel. With its 215 residues, NanC belongs to the family of small monomeric KdgM-related porins. KdgM homologues are found in gammaproteobacteria, including major plant and human pathogens, and together they define a large family of putative acidic sugar/oligosaccharide transporters, which are as yet poorly characterized. Here, we present the first high-resolution structure of a KdgM family member. NanC folds into a 28-A-high, 12-stranded beta-barrel, resembling the beta-domain of autotransporter NalP and defining an open pore with an average radius of 3.3 A. The channel is lined by two strings of basic residues facing each other across the pore, a feature that appears largely conserved within the KdgM family and is likely to facilitate the diffusion of acidic oligosaccharides.
Authors:
Christophe Wirth; Guy Condemine; C??line Boiteux; Simon Bern??che; Tilman Schirmer; Caroline M Peneff
Related Documents :
1451905 - Rat erythrocyte glycophorins can be isolated by the lithium diiodosalicylate method use...
1060425 - Heterogeneity of carcinoembryonic antigen. ii. monosaccharide composition of concanaval...
8426115 - Characterization of a novel trans-sialidase of trypanosoma brucei procyclic trypomastig...
7106355 - Cyclic changes of sialidase in human cervical mucus.
16635105 - Attenuation of abnormalities in the lipid metabolism during experimental myocardial inf...
23530225 - Substrate selectivity in glutamate-dependent acid resistance in enteric bacteria.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-09-29
Journal Detail:
Title:  Journal of molecular biology     Volume:  394     ISSN:  1089-8638     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2009-11-25     Completed Date:  2009-12-21     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  718-31     Citation Subset:  IM    
Affiliation:
Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
Data Bank Information
Bank Name/Acc. No.:
PDB/2WJQ;  2WJR
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Outer Membrane Proteins / chemistry*
Crystallography, X-Ray
Escherichia coli K12 / chemistry*
Escherichia coli Proteins / chemistry*
Models, Molecular
Molecular Sequence Data
Porins / chemistry*
Protein Structure, Tertiary
Sequence Alignment
Chemical
Reg. No./Substance:
0/Bacterial Outer Membrane Proteins; 0/Escherichia coli Proteins; 0/NanC protein, E coli; 0/Porins

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


Previous Document:  Structural and functional characterisation of the fork head transcription factor-encoding gene, Hc-d...
Next Document:  Minimal Gene Regulatory Circuits that Can Count like Bacteriophage Lambda.