4CC4

Complex of InlC of Listeria monocytogenes and human Tuba C-terminal SH3 domain

4CC4 の概要

• エントリーDOI: 10.2210/pdb4cc4/pdb
• 関連するPDBエントリー: 4CC2 4CC3
• 分子名称: INLC PROTEIN, DYNAMIN-BINDING PROTEIN, GLYCEROL, ... (9 entities in total)
• 機能のキーワード: cell invasion, bacterial infection, pathogenesis, listerial cell-cell spread, virulence factor, protein-protein interactions, leucine-rich repeat, src homology 3 domain, disruption of cortical tension, cell membrane protrusions
• 由来する生物種: LISTERIA MONOCYTOGENES EGD-E; 詳細
• 細胞内の位置: Cytoplasm : Q6XZF7
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 113900.38

構造登録者

Polle, L.,Rigano, L.,Julian, R.,Ireton, K.,Schubert, W.-D. (登録日: 2013-10-17, 公開日: 2013-10-30, 最終更新日: 2023-12-20)

主引用文献

Polle, L.,Rigano, L.A.,Julian, R.,Ireton, K.,Schubert, W.
Structural Details of Human Tuba Recruitment by Inlc of Listeria Monocytogenes Elucidate Bacterial Cell-Cell Spreading.
Structure, 22:304-, 2014

PubMed Abstract: The human pathogen Listeria monocytogenes is able to directly spread to neighboring cells of host tissues, a process recently linked to the virulence factor InlC. InlC targets the sixth SH3 domain (SH3-6) of human Tuba, disrupting its physiological interaction with the cytoskeletal protein N-WASP. The resulting loss of cortical actin tension may slacken the junctional membrane, allowing protrusion formation by motile Listeria. Complexes of Tuba SH3-6 with physiological partners N-WASP and Mena reveal equivalent binding modes but distinct affinities. The interaction surface of the infection complex InlC/Tuba SH3-6 is centered on phenylalanine 146 of InlC stacking upon asparagine 1569 of Tuba. Replacing Phe146 by alanine largely abrogates molecular affinity and in vivo mimics deletion of inlC. Collectively, our findings indicate that InlC hijacks Tuba through its LRR domain, blocking the peptide binding groove to prevent recruitment of its physiological partners.

PubMed: 24332715
DOI: 10.1016/J.STR.2013.10.017

実験手法

X-RAY DIFFRACTION (2.6 Å)