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1.55 Å resolution X‐ray crystal structure of Rv3902c from Mycobacterium tuberculosis
Author(s) -
Reddy Bharat G.,
Moates Derek B.,
Kim HeungBok,
Green Todd J.,
Kim ChangYub,
Terwilliger Thomas C.,
DeLucas Lawrence J.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14003793
Subject(s) - antiparallel (mathematics) , operon , mycobacterium tuberculosis , homology (biology) , crystallography , crystal structure , chemistry , structural genomics , gene , biology , protein structure , tuberculosis , genetics , biochemistry , physics , escherichia coli , medicine , quantum mechanics , pathology , magnetic field
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.