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Publication Abstract from PubMed
Gene rv0802c from Mycobacterium tuberculosis encodes a 218-amino-acid protein and is annotated as a hypothetical protein with homology to GCN5-related N-acetyltransferases. The structure of Rv0802c was determined in an unliganded form to 2.0 A resolution utilizing single-wavelength anomalous dispersion from a samarium soak that resulted in a single bound Sm(3+):citrate(2) complex. The structure confirms that Rv0802c exhibits the GCN5-related N-acetyltransferase fold and revealed a tetramer composed of a dimer of dimers with approximate 222 symmetry. In addition, a bound acetate ion indicated that Rv0802c may utilize a unique acyl donor for the family. The subsequent determination of the structure of Rv0802c in complex with succinyl-CoA to 2.3 A resolution suggests that Rv0802c is the first known GCN5-related N-acetyltransferase family member to utilize succinyl-CoA as a substrate.
Rv0802c from Mycobacterium tuberculosis: the first structure of a succinyltransferase with the GNAT fold.,Vetting MW, Errey JC, Blanchard JS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt, 11):978-85. Epub 2008 Oct 31. PMID:18997321[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Vetting MW, Errey JC, Blanchard JS. Rv0802c from Mycobacterium tuberculosis: the first structure of a succinyltransferase with the GNAT fold. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt, 11):978-85. Epub 2008 Oct 31. PMID:18997321 doi:10.1107/S1744309108031679
