4PR7
KdgM porin in complex with disordered oligogalacturonate
4PR7 の概要
エントリーDOI | 10.2210/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: 24914987DOI: 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) |
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