7B9F

Structure of the mycobacterial ESX-5 Type VII Secretion System hexameric pore complex

7B9F の概要

• エントリーDOI: 10.2210/pdb7b9f/pdb
• 関連するPDBエントリー: 7B9S
• EMDBエントリー: 12103 12105 12674
• 分子名称: EccE5, EccD5, EccC5, ... (4 entities in total)
• 機能のキーワード: mycobacterial esx-5 type vii secretion system, transport protein
• 由来する生物種: Mycobacterium xenopi RIVM700367; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 357440.43

構造登録者

Chojnowski, G.,Ritter, C.,Beckham, K.S.H.,Mullapudi, E.,Rettel, M.,Savitski, M.M.,Mortensen, S.A.,Ziemianowicz, D.,Kosinski, J.,Wilmanns, M. (登録日: 2020-12-14, 公開日: 2021-07-07, 最終更新日: 2024-05-01)

主引用文献

Beckham, K.S.H.,Ritter, C.,Chojnowski, G.,Ziemianowicz, D.S.,Mullapudi, E.,Rettel, M.,Savitski, M.M.,Mortensen, S.A.,Kosinski, J.,Wilmanns, M.
Structure of the mycobacterial ESX-5 type VII secretion system pore complex.
Sci Adv, 7:-, 2021

PubMed Abstract: The ESX-5 type VII secretion system is a membrane-spanning protein complex key to the virulence of mycobacterial pathogens. However, the overall architecture of the fully assembled translocation machinery and the composition of the central secretion pore have remained unknown. Here, we present the high-resolution structure of the 2.1-megadalton ESX-5 core complex. Our structure captured a dynamic, secretion-competent conformation of the pore within a well-defined transmembrane section, sandwiched between two flexible protein layers at the cytosolic entrance and the periplasmic exit. We propose that this flexibility endows the ESX-5 machinery with large conformational plasticity required to accommodate targeted protein secretion. Compared to known secretion systems, a highly dynamic state of the pore may represent a fundamental principle of bacterial secretion machineries.

PubMed: 34172453
DOI: 10.1126/sciadv.abg9923

実験手法

ELECTRON MICROSCOPY (3 Å)