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

Cohen Gonsaud, M. and Barthe, P. and Bagneris, Claire and Henderson, B. and Ward, J.M. and Roumestand, C. and Keep, Nicholas H. (2005) The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes. Nature Structural and Molecular Biology 12 (3), pp. 270-273. ISSN 1545-9993.

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Official URL: http://dx.doi.org/10.1038/nsmb905

Abstract

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.

Item Type: Article
Keyword(s) / Subject(s): RPF, NMR, Resuscitation promoting factors, Mycobacterium tuberculosis, dormant culture, bacterial cytokine
School or Research Centre: Birkbeck Schools and Research Centres > School of Science > Biological Sciences
Depositing User: Administrator
Date Deposited: 22 Mar 2006
Last Modified: 17 Apr 2013 12:32
URI: http://eprints.bbk.ac.uk/id/eprint/343

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