3LT3

Crystal structure of Rv3671c from M. tuberculosis H37Rv, Ser343Ala mutant, inactive form

Summary for 3LT3

• Entry DOI: 10.2210/pdb3lt3/pdb
• Related: 3K6Y 3K6Z
• Descriptor: POSSIBLE MEMBRANE-ASSOCIATED SERINE PROTEASE (2 entities in total)
• Functional Keywords: serine protease, h37rv, htra, hydrolase, protease
• Biological source: Mycobacterium tuberculosis H37Rv
• Total number of polymer chains: 2
• Total formula weight: 44143.89

Authors

Biswas, T.,Small, J.,Vandal, O.,Ehrt, S.,Tsodikov, O.V. (deposition date: 2010-02-14, release date: 2010-11-03, Last modification date: 2023-09-06)

Primary citation

Biswas, T.,Small, J.,Vandal, O.,Odaira, T.,Deng, H.,Ehrt, S.,Tsodikov, O.V.
Structural insight into serine protease Rv3671c that Protects M. tuberculosis from oxidative and acidic stress.
Structure, 18:1353-1363, 2010

PubMed 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 biochemical studies confirm that activation of the protease in an oxidative environment is dependent on this reversible disulfide bond. These results suggest that the disulfide bond modulates activity of Rv3671c depending on the oxidative environment in vivo.

PubMed: 20947023
DOI: 10.1016/j.str.2010.06.017

Experimental method

X-RAY DIFFRACTION (2.1 Å)