2VZZ

Crystal structure of Rv0802c from Mycobacterium tuberculosis in Complex with Succinyl-CoA

Summary for 2VZZ

• Entry DOI: 10.2210/pdb2vzz/pdb
• Related: 2VZY
• Descriptor: RV0802C, SUCCINYL-COENZYME A (3 entities in total)
• Functional Keywords: gcn5-related n-acetyltransferase, mycobacterium tuberculosis, transferase, rv0802c, succinyltransferase
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Total number of polymer chains: 4
• Total formula weight: 103531.56

Authors

Vetting, M.W.,Errey, J.C.,Blanchard, J.S. (deposition date: 2008-08-07, release date: 2009-04-07, Last modification date: 2023-12-13)

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

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: 18997321
DOI: 10.1107/S1744309108031679

Experimental method

X-RAY DIFFRACTION (2.3 Å)