1XSF
Solution structure of a resuscitation promoting factor domain from Mycobacterium tuberculosis
Summary for 1XSF
Entry DOI | 10.2210/pdb1xsf/pdb |
NMR Information | BMRB: 6221 |
Descriptor | Probable resuscitation-promoting factor rpfB (1 entity in total) |
Functional Keywords | lysozyme-like structure, cell cycle, hydrolase |
Biological source | Mycobacterium tuberculosis |
Total number of polymer chains | 1 |
Total formula weight | 11357.57 |
Authors | Cohen-Gonsaud, M.,Barthe, P.,Henderson, B.,Ward, J.,Roumestand, C.,Keep, N.H. (deposition date: 2004-10-19, release date: 2005-02-15, Last modification date: 2024-11-06) |
Primary citation | Cohen-Gonsaud, M.,Barthe, P.,Bagneris, C.,Henderson, B.,Ward, J.,Roumestand, C.,Keep, N.H. The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes Nat.Struct.Mol.Biol., 12:270-273, 2005 Cited by PubMed 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. PubMed: 15723078DOI: 10.1038/nsmb905 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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