Reddy Bharat G, Moates Derek B, Kim Heung-Bok, Green Todd J, Kim Chang-Yub, Terwilliger Thomas C, DeLucas Lawrence J
Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35233, USA.
Department of Biology, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35233, USA.
Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):414-7. doi: 10.1107/S2053230X14003793. Epub 2014 Mar 25.
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.
结核分枝杆菌(TB)蛋白Rv3902c(176个残基;分子量为19.8 kDa)的晶体结构在1.55 Å分辨率下得以确定。尽管参与细菌致病机制的几个结核分枝杆菌基因是从包含Rv3902c基因的操纵子中表达的,但Rv3902c的功能尚不清楚。Rv3902c独特的结构折叠包含两个结构域,每个结构域由反平行β折叠和α螺旋组成,在手掌部位形成一个带有小结合口袋的手状结合基序。结构同源性搜索表明,Rv3902c的整体结构与沙门氏菌毒力因子伴侣蛋白InvB相似,在对齐结构域中的主链原子的均方根偏差为2.3 Å。