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1F02

CRYSTAL STRUCTURE OF C-TERMINAL 282-RESIDUE FRAGMENT OF INTIMIN IN COMPLEX WITH TRANSLOCATED INTIMIN RECEPTOR (TIR) INTIMIN-BINDING DOMAIN

1F02 の概要
エントリーDOI10.2210/pdb1f02/pdb
関連するPDBエントリー1CWV 1F00 1INM
分子名称INTIMIN, TRANSLOCATED INTIMIN RECEPTOR (2 entities in total)
機能のキーワードimmunoglobulin-like fold, c-type lectin-like fold, four-helix bundle, cell adhesion
由来する生物種Escherichia coli
詳細
細胞内の位置Cell outer membrane; Single-pass membrane protein: P19809
タンパク質・核酸の鎖数2
化学式量合計37143.12
構造登録者
Luo, Y.,Frey, E.A.,Pfuetzner, R.A.,Creagh, A.L.,Knoechel, D.G.,Haynes, C.A.,Finlay, B.B.,Strynadka, N.C.J. (登録日: 2000-05-14, 公開日: 2000-07-12, 最終更新日: 2024-10-16)
主引用文献Luo, Y.,Frey, E.A.,Pfuetzner, R.A.,Creagh, A.L.,Knoechel, D.G.,Haynes, C.A.,Finlay, B.B.,Strynadka, N.C.
Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex.
Nature, 405:1073-1077, 2000
Cited by
PubMed Abstract: Intimin and its translocated intimin receptor (Tir) are bacterial proteins that mediate adhesion between mammalian cells and attaching and effacing (A/E) pathogens. Enteropathogenic Escherichia coli (EPEC) causes significant paediatric morbidity and mortality world-wide. A related A/E pathogen, enterohaemorrhagic E. coli (EHEC; O157:H7) is one of the most important food-borne pathogens in North America, Europe and Japan. A unique and essential feature of A/E bacterial pathogens is the formation of actin-rich pedestals beneath the intimately adherent bacteria and localized destruction of the intestinal brush border. The bacterial outer membrane adhesin, intimin, is necessary for the production of the A/E lesion and diarrhoea. The A/E bacteria translocate their own receptor for intimin, Tir, into the membrane of mammalian cells using the type III secretion system. The translocated Tir triggers additional host signalling events and actin nucleation, which are essential for lesion formation. Here we describe the the crystal structures of an EPEC intimin carboxy-terminal fragment alone and in complex with the EPEC Tir intimin-binding domain, giving insight into the molecular mechanisms of adhesion of A/E pathogens.
PubMed: 10890451
DOI: 10.1038/35016618
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.9 Å)
構造検証レポート
Validation report summary of 1f02
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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