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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism
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Bacterial Proteins / physiology
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Binding Sites
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Cytokines / chemistry*
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Cytokines / metabolism
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Cytokines / physiology
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Glutamic Acid / chemistry
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Glycoside Hydrolases / chemistry*
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Magnetic Resonance Spectroscopy
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Muramidase / chemistry
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Mycobacterium tuberculosis / metabolism*
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Protein Structure, Tertiary
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Solutions / chemistry
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Structural Homology, Protein
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Trisaccharides / chemistry
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Trisaccharides / metabolism
Substances
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Bacterial Proteins
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Cytokines
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Solutions
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Trisaccharides
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resuscitation-promoting factor, bacteria
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N,N',N''-triacetylchitotriose
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Glutamic Acid
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Glycoside Hydrolases
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Muramidase