1.55 Å resolution X-ray crystal structure of Rv3902c from Mycobacterium tuberculosis.
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.
Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35233, USA.
Bharat G
BG
Reddy
Department of Biology, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35233, USA.
Derek B
DB
Moates
Bioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Heung-Bok
HB
Kim
Department of Microbiology, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35233, USA.
Todd J
TJ
Green
Bioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Chang-Yub
CY
Kim
Bioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Thomas C
TC
Terwilliger
Department of Optometry, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35233, USA.
Lawrence J
LJ
DeLucas
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D008958:Models, Molecular; D009169:Mycobacterium tuberculosis / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding
D001426:Bacterial Proteins
Mycobacterium tuberculosis; Rv3902c; novel fold; virulence-factor chaperone