来自结核分枝杆菌的复苏促进因子结构域的结构显示出与溶菌酶的同源性。
The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes.
作者信息
Cohen-Gonsaud Martin, Barthe Philippe, Bagnéris Claire, Henderson Brian, Ward John, Roumestand Christian, Keep Nicholas H
机构信息
School of Crystallography and Institute for Structural Molecular Biology, Birkbeck College, University of London, Malet Street, London, WC1E 7HX, UK.
出版信息
Nat Struct Mol Biol. 2005 Mar;12(3):270-3. doi: 10.1038/nsmb905. Epub 2005 Feb 20.
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.
复苏促进因子（RPF）蛋白可使富含（G+C）的革兰氏阳性菌的稳定期培养物重新活化，其中包括结核病病原体结核分枝杆菌。我们报告了通过异核多维核磁共振解析的结核分枝杆菌Rv1009（RpfB）的RPF结构域的溶液结构。与各种糖苷水解酶的结构同源性表明RpfB可切割寡糖。生化研究表明，保守的活性位点谷氨酸对于复苏活性很重要。这些数据以及存在一个明显的大分子结合口袋表明，寡糖切割可能是从休眠中复苏的信号。
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