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Article Dans Une Revue Nature Structural and Molecular Biology Année : 2005

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

Résumé

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.

Dates et versions

hal-03472337 , version 1 (09-12-2021)

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Martin Cohen-Gonsaud, Philippe Barthe, Claire Bagnéris, Brian Henderson, John Ward, et al.. The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes. Nature Structural and Molecular Biology, 2005, 12 (3), pp.270-273. ⟨10.1038/nsmb905⟩. ⟨hal-03472337⟩
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