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.
Original language | English (US) |
---|---|
Pages (from-to) | 978-985 |
Number of pages | 8 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 64 |
Issue number | 11 |
DOIs | |
State | Published - 2008 |
Externally published | Yes |
Keywords
- GCN5-related N-acetyltransferases
- Mycobacterium tuberculosis
- Rv0802c
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics