Open AccessRv0802c from Mycobacterium tuberculosis : the first structure of a succinyltransferase with the GNAT fold
Author(s) -
Vetting Matthew W.,
Errey James C.,
Blanchard John S.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108031679
Subject(s) - acetyltransferase , dimer , mycobacterium tuberculosis , acetyltransferases , chemistry , homology (biology) , crystallography , stereochemistry , biology , amino acid , gene , biochemistry , tuberculosis , acetylation , medicine , pathology , organic chemistry
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 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 Å resolution suggests that Rv0802c is the first known GCN5‐related N ‐acetyltransferase family member to utilize succinyl‐CoA as a substrate.