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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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.
Metadata
| Item Type: | Article |
|---|---|
| Keyword(s) / Subject(s): | RPF, NMR, Resuscitation promoting factors, Mycobacterium tuberculosis, dormant culture, bacterial cytokine |
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Research Centres and Institutes: | Structural Molecular Biology, Institute of (ISMB) |
| Depositing User: | Administrator |
| Date Deposited: | 22 Mar 2006 |
| Last Modified: | 02 Aug 2023 16:46 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/343 |
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