Structural insight into serine protease Rv3671c that Protects M. tuberculosis from oxidative and acidic stress.

ABSTRACT: Rv3671c, a putative serine protease, is crucial for persistence of Mycobacterium tuberculosis in the hostile environment of the phagosome. We show that Rv3671c is required for M. tuberculosis resistance to oxidative stress in addition to its role in protection from acidification. Structural and biochemical analyses demonstrate that the periplasmic domain of Rv3671c is a functional serine protease of the chymotrypsin family and, remarkably, that its activity increases on oxidation. High-resolution crystal structures of this protease in an active strained state and in an inactive relaxed state reveal that a solvent-exposed disulfide bond controls the protease activity by constraining two distant regions of Rv3671c and stabilizing it in the catalytically active conformation. In vitro biochemi

SUBMITTER: Biswas T 

PROVIDER: S-EPMC2955984 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature