The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes

被引：128

作者：

Cohen-Gonsaud, M

Barthe, P

Bagnéris, C

Henderson, B

Ward, J

Roumestand, C

Keep, NH

机构：

[1] Univ London Birkbeck Coll, Sch Crystallogr, London WC1E 7HX, England

[2] Univ London Birkbeck Coll, Inst Struct Mol Biol, London WC1E 7HX, England

[3] UMI, Ctr Biochim Struct, CNRS,Fac Pharm,UMR554, INSERM,UMR5048, F-34093 Montpellier 5, France

[4] UCL, Div Microbial Dis, Eastman Dent Inst, London WC1X 8LD, England

[5] UCL, Dept Biochem & Mol Biol, London WC1E 6BT, England

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2005年 / 12卷 / 03期

关键词：

D O I：

10.1038/nsmb905

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Resuscitation- promoting factor (RPF) proteins reactivate stationary-phase cultures of (G+C)- rich Gram-positive bacteria including the causative agent of tuberculosis, Mycobacterium tuberculosis. We report the solution structure of the RPF domain from M. tuberculosis Rv1009 (RpfB) solved by heteronuclear multidimensional NMR. Structural homology with various glycoside hydrolases suggested that RpfB cleaved oligosaccharides. Biochemical studies indicate that a conserved active site glutamate is important for resuscitation activity. These data, as well as the presence of a clear binding pocket for a large molecule, indicate that oligosaccharide cleavage is probably the signal for revival from dormancy.

引用

页码：270 / 273

页数：4