2WJQ

NanC porin structure in hexagonal crystal form.

2WJQ の概要

• エントリーDOI: 10.2210/pdb2wjq/pdb
• 関連するPDBエントリー: 2WJR
• 分子名称: PROBABLE N-ACETYLNEURAMINIC ACID OUTER MEMBRANE CHANNEL PROTEIN NANC, CHLORIDE ION, N-OCTANE, ... (5 entities in total)
• 機能のキーワード: kdgm family, beta-barrel, monomeric porin, transport protein, outer membrane protein, sialic acid translocation
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27506.52

構造登録者

Wirth, C.,Condemine, G.,Schirmer, T.,Peneff, C.M. (登録日: 2009-05-28, 公開日: 2009-10-13, 最終更新日: 2024-05-08)

主引用文献

Wirth, C.,Condemine, G.,Boiteux, C.,Berneche, S.,Schirmer, T.,Peneff, C.M.
Nanc Crystal Structure, a Model for Outer Membrane Channels of the Acidic Sugar-Specific Kdgm Porin Family.
J.Mol.Biol., 394:718-, 2009

PubMed 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-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.

PubMed: 19796645
DOI: 10.1016/J.JMB.2009.09.054

実験手法

X-RAY DIFFRACTION (2 Å)