Unknown

Dataset Information

0

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


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.

SUBMITTER: Vetting MW 

PROVIDER: S-EPMC2581710 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Vetting Matthew W MW   Errey James C JC   Blanchard John S JS  

Acta crystallographica. Section F, Structural biology and crystallization communications 20081031 Pt 11


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 compo  ...[more]

Similar Datasets

| S-EPMC2323992 | biostudies-literature
| S-EPMC4738035 | biostudies-literature
| S-EPMC1951255 | biostudies-literature
| S-EPMC6949403 | biostudies-literature
| S-EPMC2531272 | biostudies-literature
| S-EPMC1855508 | biostudies-literature
| S-EPMC6022014 | biostudies-literature
| S-EPMC3561247 | biostudies-literature
| S-EPMC1276712 | biostudies-literature
| S-EPMC2651758 | biostudies-literature