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

被引：1
|
作者：
Reddy, Bharat G. [1 ]
Moates, Derek B. [2 ]
Kim, Heung-Bok [3 ]
Green, Todd J. [4 ]
Kim, Chang-Yub [3 ]
Terwilliger, Thomas C. [3 ]
DeLucas, Lawrence J. [5 ]
机构：
[1] Univ Alabama Birmingham, Dept Biochem & Mol Genet, Birmingham, AL 35233 USA
[2] Univ Alabama Birmingham, Dept Biol, Birmingham, AL 35233 USA
[3] Los Alamos Natl Lab, Biosci Div, Los Alamos, NM 87545 USA
[4] Univ Alabama Birmingham, Dept Microbiol, Birmingham, AL 35233 USA
[5] Univ Alabama Birmingham, Dept Optometry, Birmingham, AL 35233 USA
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2014年 / 70卷
关键词：
VIRULENCE; PROTEINS; COMPLEX; MODEL;
D O I：
10.1107/S2053230X14003793
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The crystallographic structure of the Mycobacterium tuberculosis (TB) protein Rv3902c (176 residues; molecular mass of 19.8 kDa) was determined at 1.55 angstrom 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 angstrom along an aligned domain.
引用
收藏
页码：414 / 417
页数：4
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