2VZY
Crystal structure of Rv0802c from Mycobacterium tuberculosis in an unliganded form.
Summary for 2VZY
| Entry DOI | 10.2210/pdb2vzy/pdb |
| Related | 2VZZ |
| Descriptor | RV0802C, ACETATE ION, SULFATE ION, ... (7 entities in total) |
| Functional Keywords | transferase, gcn5-related n-acetyltransferase, mycobacterium tuberculosis, rv0802c, succinyltransferase |
| Biological source | MYCOBACTERIUM TUBERCULOSIS |
| Total number of polymer chains | 4 |
| Total formula weight | 101660.72 |
| Authors | Vetting, M.W.,Errey, J.C.,Blanchard, J.S. (deposition date: 2008-08-07, release date: 2009-04-07, Last modification date: 2024-05-08) |
| Primary citation | Vetting, M.W.,Errey, J.C.,Blanchard, J.S. Rv0802C from Mycobacterium Tuberculosis: The First Structure of a Succinyltransferase with the Gnat Fold. Acta Crystallogr.,Sect.F, 64:978-, 2008 Cited by PubMed Abstract: 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. PubMed: 18997321DOI: 10.1107/S1744309108031679 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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