4O6G

Rv3902c from M. tuberculosis

Summary for 4O6G

• Entry DOI: 10.2210/pdb4o6g/pdb
• Descriptor: Uncharacterized protein (2 entities in total)
• Functional Keywords: structural genomics, niaid, national institute of allergy and infectious diseases, tb structural genomics consortium, tbsgc, unknown function
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 19546.97

Authors

Reddy, B.G.,Moates, D.B.,Kim, H.,Green, T.J.,Kim, C.,Terwilliger, T.J.,Delucas, L.J.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2013-12-20, release date: 2014-03-05, Last modification date: 2024-04-03)

Primary citation

Reddy, B.G.,Moates, D.B.,Kim, H.B.,Green, T.J.,Kim, C.Y.,Terwilliger, T.C.,Delucas, L.J.
1.55 angstrom resolution X-ray crystal structure of Rv3902c from Mycobacterium tuberculosis.
Acta Crystallogr F Struct Biol Commun, 70:414-417, 2014

PubMed Abstract: 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.

PubMed: 24699730
DOI: 10.1107/S2053230X14003793

Experimental method

X-RAY DIFFRACTION (1.55 Å)