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Rv0802c from Mycobacterium tuberculosis: the first structure of a succinyltransferase with the GNAT fold.

Authors :
Vetting, Matthew W.
Errey, James C.
Blanchard, John S.
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]

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