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Article
Nature Structural & Molecular Biology  12, 270 - 273 (2005)
Published online: 20 February 2005; | doi:10.1038/nsmb905

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

Martin Cohen-Gonsaud1, Philippe Barthe2, Claire Bagnéris1, Brian Henderson3, John Ward4, Christian Roumestand2 & Nicholas H Keep1

1  School of Crystallography and Institute for Structural Molecular Biology, Birkbeck College, University of London, Malet Street, London, WC1E 7HX, UK.

2  Centre de Biochimie Structurale, CNRS UMR5048, INSERM UMR554, UMI, Faculté de Pharmacie, BP 14491, 15 Avenue Charles Flahault, 34093 Montpellier Cedex 5, France.

3  Division of Microbial Diseases, Eastman Dental Institute, University College London, 256 Gray's Inn Road, London WC1X 8LD, UK.

4  Department of Biochemistry and Molecular Biology, University College London, Gower Street, London WC1E 6BT, UK.

Correspondence should be addressed to Nicholas H Keep n.keep@mail.cryst.bbk.ac.uk
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.

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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