5XUR

Crystal Structure of Rv2466c C22S Mutant

Summary for 5XUR

• Entry DOI: 10.2210/pdb5xur/pdb
• Descriptor: Thioredoxin-like reductase Rv2466c, 1,2-ETHANEDIOL, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: thioredoxin-like, oxidoreductase
• Biological source: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
• Cellular location: Cytoplasm : O53193
• Total number of polymer chains: 4
• Total formula weight: 96575.87

Authors

Zhang, X.,Li, H. (deposition date: 2017-06-25, release date: 2018-03-14, Last modification date: 2023-11-22)

Primary citation

Negri, A.,Javidnia, P.,Mu, R.,Zhang, X.,Vendome, J.,Gold, B.,Roberts, J.,Barman, D.,Ioerger, T.,Sacchettini, J.C.,Jiang, X.,Burns-Huang, K.,Warrier, T.,Ling, Y.,Warren, J.D.,Oren, D.A.,Beuming, T.,Wang, H.,Wu, J.,Li, H.,Rhee, K.Y.,Nathan, C.F.,Liu, G.,Somersan-Karakaya, S.
Identification of a Mycothiol-Dependent Nitroreductase from Mycobacterium tuberculosis.
ACS Infect Dis, 4:771-787, 2018

PubMed Abstract: The success of Mycobacterium tuberculosis (Mtb) as a pathogen depends on the redundant and complex mechanisms it has evolved for resisting nitrosative and oxidative stresses inflicted by host immunity. Improving our understanding of these defense pathways can reveal vulnerable points in Mtb pathogenesis. In this study, we combined genetic, structural, computational, biochemical, and biophysical approaches to identify a novel enzyme class represented by Rv2466c. We show that Rv2466c is a mycothiol-dependent nitroreductase of Mtb and can reduce the nitro group of a novel mycobactericidal compound using mycothiol as a cofactor. In addition to its function as a nitroreductase, Rv2466c confers partial protection to menadione stress.

PubMed: 29465985
DOI: 10.1021/acsinfecdis.7b00111

Experimental method

X-RAY DIFFRACTION (1.996 Å)