4KPG

Crystal structure of MycP1 from the ESX-1 type VII secretion system

4KPG の概要

• エントリーDOI: 10.2210/pdb4kpg/pdb
• 関連するPDBエントリー: 4J94
• 分子名称: Membrane-anchored mycosin mycp1 (2 entities in total)
• 機能のキーワード: subtilisin, protease, hydrolase
• 由来する生物種: Mycobacterium smegmatis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42153.75

構造登録者

Solomonson, M.,Wasney, G.A.,Watanabe, N.,Gruninger, R.J.,Prehna, G.,Strynadka, N.C.J. (登録日: 2013-05-13, 公開日: 2013-05-22, 最終更新日: 2024-10-16)

主引用文献

Solomonson, M.,Huesgen, P.F.,Wasney, G.A.,Watanabe, N.,Gruninger, R.J.,Prehna, G.,Overall, C.M.,Strynadka, N.C.
Structure of the Mycosin-1 Protease from the Mycobacterial ESX-1 Protein Type VII Secretion System.
J.Biol.Chem., 288:17782-17790, 2013

PubMed Abstract: Mycobacteria use specialized type VII (ESX) secretion systems to export proteins across their complex cell walls. Mycobacterium tuberculosis encodes five nonredundant ESX secretion systems, with ESX-1 being particularly important to disease progression. All ESX loci encode extracellular membrane-bound proteases called mycosins (MycP) that are essential to secretion and have been shown to be involved in processing of type VII-exported proteins. Here, we report the first x-ray crystallographic structure of MycP1(24-407) to 1.86 Å, defining a subtilisin-like fold with a unique N-terminal extension previously proposed to function as a propeptide for regulation of enzyme activity. The structure reveals that this N-terminal extension shows no structural similarity to previously characterized protease propeptides and instead wraps intimately around the catalytic domain where, tethered by a disulfide bond, it forms additional interactions with a unique extended loop that protrudes from the catalytic core. We also show MycP1 cleaves the ESX-1 secreted protein EspB from both M. tuberculosis and Mycobacterium smegmatis at a homologous cut site in vitro.

PubMed: 23620593
DOI: 10.1074/jbc.M113.462036

実験手法

X-RAY DIFFRACTION (2.148 Å)