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4PR7

KdgM porin in complex with disordered oligogalacturonate

4PR7 の概要
エントリーDOI10.2210/pdb4pr7/pdb
関連するPDBエントリー4FQE
分子名称Oligogalacturonate-specific porin KdgM, alpha-D-galactopyranuronic acid-(1-4)-alpha-D-galactopyranuronic acid-(1-4)-alpha-D-galactopyranuronic acid-(1-4)-alpha-D-galactopyranuronic acid-(1-4)-alpha-D-galactopyranuronic acid, N-OCTANE, ... (5 entities in total)
機能のキーワードbeta barrel, oligogalacturonate specificity, transport protein, outer membrane protein
由来する生物種Dickeya dadantii
細胞内の位置Cell outer membrane: Q934G3
タンパク質・核酸の鎖数1
化学式量合計27514.43
構造登録者
Hutter, C.,Peneff, C.M.,Wirth, C.,Schirmer, T. (登録日: 2014-03-05, 公開日: 2014-06-11, 最終更新日: 2023-09-20)
主引用文献Hutter, C.A.,Lehner, R.,Wirth, C.h.,Condemine, G.,Peneff, C.,Schirmer, T.
Structure of the oligogalacturonate-specific KdgM porin.
Acta Crystallogr.,Sect.D, 70:1770-1778, 2014
Cited by
PubMed Abstract: The phytopathogenic Gram-negative bacterium Dickeya dadantii (Erwinia chrysanthemi) feeds on plant cell walls by secreting pectinases and utilizing the oligogalacturanate products. An outer membrane porin, KdgM, is indispensable for the uptake of these acidic oligosaccharides. Here, the crystal structure of KdgM determined to 1.9 Å resolution is presented. KdgM is folded into a regular 12-stranded antiparallel β-barrel with a circular cross-section defining a transmembrane pore with a minimal radius of 3.1 Å. Most of the loops that would face the cell exterior in vivo are disordered, but nevertheless mediate contact between densely packed membrane-like layers in the crystal. The channel is lined by two tracks of arginine residues facing each other across the pore, a feature that is conserved within the KdgM family and is likely to facilitate the diffusion of acidic oligosaccharides.
PubMed: 24914987
DOI: 10.1107/S1399004714007147
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.1 Å)
構造検証レポート
Validation report summary of 4pr7
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-23に公開中

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