2WQV

Internalin domain of Listeria monocytogenes InlB: rhombohedral crystal form

2WQV の概要

• エントリーDOI: 10.2210/pdb2wqv/pdb
• 関連するPDBエントリー: 1D0B 1H6T 1M9S 1OTM 1OTN 1OTO 2UZX 2UZY 2WQU 2WQW 2WQX
• 分子名称: INTERNALIN B, TETRAETHYLENE GLYCOL, TRIETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: hgf receptor ligand, leucine-rich repeat, lrr, c-met ligand, cell invasion, virulence factor
• 由来する生物種: LISTERIA MONOCYTOGENES
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65476.78

構造登録者

Niemann, H.H.,Heinz, D.W. (登録日: 2009-08-27, 公開日: 2009-11-10, 最終更新日: 2023-12-20)

主引用文献

Ferraris, D.M.,Gherardi, E.,Di, Y.,Heinz, D.W.,Niemann, H.H.
Ligand-Mediated Dimerization of the met Receptor Tyrosine Kinase by the Bacterial Invasion Protein Inlb.
J.Mol.Biol., 395:522-, 2010

PubMed Abstract: The Listeria monocytogenes surface protein InlB mediates bacterial invasion into host cells by activating the human receptor tyrosine kinase Met. So far, it is unknown how InlB or the physiological Met ligand hepatocyte growth factor/scatter factor causes Met dimerization, which is considered a prerequisite for receptor activation. We determined two new structures of InlB, revealing a recurring, antiparallel, dimeric arrangement, in which the two protomers interact through the convex face of the leucine-rich repeat domain. The same contact is found in one structure of the InlB-Met complex. Mutations disrupting the interprotomeric contact of InlB reduced its ability to activate Met and downstream signaling. Conversely, stabilization of this crystal contact by two intermolecular disulfide bonds generates a constitutively dimeric InlB variant with exceptionally high signaling activity, which can stimulate cell motility and cell division. These data demonstrate that the signaling-competent InlB-Met complex assembles with 2:2 stoichiometry around a back-to-back InlB dimer, enabling the direct contact between the stalk region of two Met molecules.

PubMed: 19900460
DOI: 10.1016/J.JMB.2009.10.074

実験手法

X-RAY DIFFRACTION (2.8 Å)