1M9S

Crystal structure of Internalin B (InlB), a Listeria monocytogenes virulence protein containing SH3-like domains.

1M9S の概要

• エントリーDOI: 10.2210/pdb1m9s/pdb
• 関連するPDBエントリー: 1CKA 1D0B 1H6T 1H6U 2ABL
• 分子名称: Internalin B, TERBIUM(III) ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: internalin, cell invasion, gw domains, sh3 domains, signaling protein
• 由来する生物種: Listeria monocytogenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 69830.62

構造登録者

Marino, M.,Banerjee, M.,Jonquieres, R.,Cossart, P.,Ghosh, P. (登録日: 2002-07-29, 公開日: 2002-11-06, 最終更新日: 2024-02-14)

主引用文献

Marino, M.,Banerjee, M.,Jonquieres, R.,Cossart, P.,Ghosh, P.
GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands
Embo J., 21:5623-5634, 2002

PubMed Abstract: InlB, a surface-localized protein of Listeria monocytogenes, induces phagocytosis in non-phagocytic mammalian cells by activating Met, a receptor tyrosine kinase. InlB also binds glycosaminoglycans and the protein gC1q-R, two additional host ligands implicated in invasion. We present the structure of InlB, revealing a highly elongated molecule with leucine-rich repeats that bind Met at one end, and GW domains that dissociably bind the bacterial surface at the other. Surprisingly, the GW domains are seen to resemble SH3 domains. Despite this, GW domains are unlikely to act as functional mimics of SH3 domains since their potential proline-binding sites are blocked or destroyed. However, we do show that the GW domains, in addition to binding glycosaminoglycans, bind gC1q-R specifically, and that this binding requires release of InlB from the bacterial surface. Dissociable attachment to the bacterial surface via the GW domains may be responsible for restricting Met activation to a small, localized area of the host cell and for coupling InlB-induced host membrane dynamics with bacterial proximity during invasion.

PubMed: 12411480
DOI: 10.1093/emboj/cdf558

実験手法

X-RAY DIFFRACTION (2.65 Å)