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CRYSTAL STRUCTURE OF RV0802C FROM MYCOBACTERIUM TUBERCULOSIS IN AN UNLIGANDED FORM.CRYSTAL STRUCTURE OF RV0802C FROM MYCOBACTERIUM TUBERCULOSIS IN AN UNLIGANDED FORM.
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGene 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
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