The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes.
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.
Cohen-Gonsaud
Martin
M
School of Crystallography and Institute for Structural Molecular Biology, Birkbeck College, University of London, Malet Street, London, WC1E 7HX, UK.
Barthe
Philippe
P
Bagnéris
Claire
C
Henderson
Brian
B
Ward
John
J
Roumestand
Christian
C
Keep
Nicholas H
NH
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D001665:Binding Sites; D016207:Cytokines / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D018698:Glutamic Acid / Q000737:chemistry; D006026:Glycoside Hydrolases / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D009113:Muramidase / Q000737:chemistry; D009169:Mycobacterium tuberculosis / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D012996:Solutions / Q000737:chemistry; D040681:Structural Homology, Protein; D014312:Trisaccharides / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D016207:Cytokines; D012996:Solutions; D014312:Trisaccharides; C113704:resuscitation-promoting factor, bacteria; C019117:N,N',N''-triacetylchitotriose; D018698:Glutamic Acid; D006026:Glycoside Hydrolases; D009113:Muramidase