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NanC Crystal Structure, a Model for Outer-Membrane Channels of the Acidic Sugar-Specific KdgM Porin Family
Authors:Christophe Wirth  Céline Boiteux  Tilman Schirmer
Institution:1 Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland
2 Université de Lyon, F-69003; Université Lyon 1, F-69622; INSA-Lyon, Villeurbanne, F-69621; CNRS, UMR5240, Microbiologie Adaptation et Pathogénie, France
3 Swiss Institute of Bioinformatics, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland
Abstract: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-Å-high, 12-stranded β-barrel, resembling the β-domain of autotransporter NalP and defining an open pore with an average radius of 3.3 Å. 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.
Keywords:OPOE  octylpolyoxyethylene  GAn  oligogalacturonate  MIRAS  multiple isomorphous replacement with anomalous scattering  LDAO  lauryldimethylamine-N-oxide  Neu5Ac  N-acetylneuraminic acid  IB-NanC  inclusion body-targeted NanC  Mb-NanC  outer membrane-targeted NanC
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