6E7E

High resolution crystal structure of IncA soluble domain

6E7E の概要

• エントリーDOI: 10.2210/pdb6e7e/pdb
• 分子名称: Inclusion membrane protein A (2 entities in total)
• 機能のキーワード: membrane fusion, chlamydia, snare-like protein, inclusion, protein binding
• 由来する生物種: Chlamydia trachomatis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19571.09

構造登録者

Cingolani, G.,Paumet, F. (登録日: 2018-07-26, 公開日: 2019-07-10, 最終更新日: 2024-03-13)

主引用文献

Cingolani, G.,McCauley, M.,Lobley, A.,Bryer, A.J.,Wesolowski, J.,Greco, D.L.,Lokareddy, R.K.,Ronzone, E.,Perilla, J.R.,Paumet, F.
Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA.
Nat Commun, 10:2747-2747, 2019

PubMed Abstract: Many intracellular bacteria, including Chlamydia, establish a parasitic membrane-bound organelle inside the host cell that is essential for the bacteria's survival. Chlamydia trachomatis forms inclusions that are decorated with poorly characterized membrane proteins known as Incs. The prototypical Inc, called IncA, enhances Chlamydia pathogenicity by promoting the homotypic fusion of inclusions and shares structural and functional similarity to eukaryotic SNAREs. Here, we present the atomic structure of the cytoplasmic domain of IncA, which reveals a non-canonical four-helix bundle. Structure-based mutagenesis, molecular dynamics simulation, and functional cellular assays identify an intramolecular clamp that is essential for IncA-mediated homotypic membrane fusion during infection.

PubMed: 31227715
DOI: 10.1038/s41467-019-10806-9

実験手法

X-RAY DIFFRACTION (1.12 Å)