1.55 Å resolution X-ray crystal structure of Rv3902c from Mycobacterium tuberculosis
- University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35233 (United States)
- Los Alamos National Laboratory, Los Alamos, NM 87545 (United States)
The 1.55 Å resolution X-ray crystal structure of Rv3902c from M. tuberculosis reveals a novel fold. The crystallographic structure of the Mycobacterium tuberculosis (TB) protein Rv3902c (176 residues; molecular mass of 19.8 kDa) was determined at 1.55 Å resolution. The function of Rv3902c is unknown, although several TB genes involved in bacterial pathogenesis are expressed from the operon containing the Rv3902c gene. The unique structural fold of Rv3902c contains two domains, each consisting of antiparallel β-sheets and α-helices, creating a hand-like binding motif with a small binding pocket in the palm. Structural homology searches reveal that Rv3902c has an overall structure similar to that of the Salmonella virulence-factor chaperone InvB, with an r.m.s.d. for main-chain atoms of 2.3 Å along an aligned domain.
- OSTI ID:
- 22375682
- Journal Information:
- Acta crystallographica. Section F, Structural biology communications, Vol. 70, Issue Pt 4; Other Information: PMCID: PMC3976054; PMID: 24699730; PUBLISHER-ID: fw5445; OAI: oai:pubmedcentral.nih.gov:3976054; Copyright (c) Reddy et al. 2014; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA); ISSN 2053-230X
- Country of Publication:
- United States
- Language:
- English
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