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Rv0802c from Mycobacterium tuberculosis: the first structure of a succinyltransferase with the GNAT fold.
- Source :
-
Acta Crystallographica: Section F (Wiley-Blackwell) . Nov2008, Vol. 64 Issue 11, p978-985. 8p. - Publication Year :
- 2008
-
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 Å resolution utilizing single-wavelength anomalous dispersion from a samarium soak that resulted in a single bound Sm3+:citrate2 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 Å resolution suggests that Rv0802c is the first known GCN5-related N-acetyltransferase family member to utilize succinyl-CoA as a substrate. [ABSTRACT FROM AUTHOR]
- Subjects :
- *MYCOBACTERIUM tuberculosis
*AMINO acids
*ACETYLTRANSFERASES
*DIMERS
*SAMARIUM
Subjects
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 64
- Issue :
- 11
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 110812046
- Full Text :
- https://doi.org/10.1107/S1744309108031679