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1.55?A resolution X-ray crystal structure of Rv3902c from Mycobacterium tuberculosis.

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 ?-sheets and ?-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.

SUBMITTER: Reddy BG 

PROVIDER: S-EPMC3976054 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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1.55 Å resolution X-ray crystal structure of Rv3902c from Mycobacterium tuberculosis.

Reddy Bharat G BG   Moates Derek B DB   Kim Heung-Bok HB   Green Todd J TJ   Kim Chang-Yub CY   Terwilliger Thomas C TC   DeLucas Lawrence J LJ  

Acta crystallographica. Section F, Structural biology communications 20140325 Pt 4

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  ...[more]

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