Structure of the mycosin-1 protease from the mycobacterial ESX-1 protein type VII secretion system.

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 pro

SUBMITTER: Solomonson M 

PROVIDER: S-EPMC3682577 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature