4o6g | pdb_00004o6g
From Proteopedia
Rv3902c from M. tuberculosis
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Structural highlights
FunctionPublication Abstract from PubMedThe crystallographic structure of the Mycobacterium tuberculosis (TB) protein Rv3902c (176 residues; molecular mass of 19.8 kDa) was determined at 1.55 A 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 beta-sheets and alpha-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 A along an aligned domain. 1.55 A resolution X-ray crystal structure of Rv3902c from Mycobacterium tuberculosis.,Reddy BG, Moates DB, Kim HB, Green TJ, Kim CY, Terwilliger TC, Delucas LJ Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):414-7. doi:, 10.1107/S2053230X14003793. Epub 2014 Mar 25. PMID:24699730[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 08:58, 18 January 2023.