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

Bharat G Reddy; Derek B Moates; Heung-Bok Kim; Todd J Green; Chang-Yub Kim; Thomas C Terwilliger; Lawrence J DeLucas

doi:10.1107/S2053230X14003793

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

Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):414-7. doi: 10.1107/S2053230X14003793. Epub 2014 Mar 25.

Authors

Bharat G Reddy¹, Derek B Moates², Heung-Bok Kim³, Todd J Green⁴, Chang-Yub Kim³, Thomas C Terwilliger³, Lawrence J DeLucas⁵

Affiliations

¹ Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35233, USA.
² Department of Biology, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35233, USA.
³ Bioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
⁴ Department of Microbiology, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35233, USA.
⁵ Department of Optometry, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35233, USA.

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.

Keywords: Mycobacterium tuberculosis; Rv3902c; novel fold; virulence-factor chaperone.

Publication types

Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Bacterial Proteins / chemistry*
Crystallization
Crystallography, X-Ray / methods*
Models, Molecular
Mycobacterium tuberculosis / chemistry*
Protein Conformation*
Protein Folding*

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

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