CRYSTAL-STRUCTURE OF A GCN5-RELATED N-ACETYLTRANSFERASE - SERRATIA-MARCESCENS AMINOGLYCOSIDE 3-N-ACETYLTRANSFERASE

Citation
E. Wolf et al., CRYSTAL-STRUCTURE OF A GCN5-RELATED N-ACETYLTRANSFERASE - SERRATIA-MARCESCENS AMINOGLYCOSIDE 3-N-ACETYLTRANSFERASE, Cell (Cambridge), 94(4), 1998, pp. 439-449
Citations number
49
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biology,"Cell Biology
Journal title
ISSN journal
0092-8674
Volume
94
Issue
4
Year of publication
1998
Pages
439 - 449
Database
ISI
SICI code
0092-8674(1998)94:4<439:COAGN->2.0.ZU;2-B
Abstract
The X-ray structure of a canonical GCN5-related N-acetyltransferase (G NAT), Serratia marcescens aminoglycoside 3-N-acetyltransferase, bound to coenzyme A (CoA) has been determined at 2.3 Angstrom resolution. Th e single domain alpha/beta protein resembles a cupped right hand wrapp ed around a cylinder and consists of a highly curved, six-stranded bet a sheet of mixed polarity that is sandwiched between four alpha helice s. The structure includes all four conserved GNAT motifs (C, D, A, and B) and represents the catalytic core of this large enzyme superfamily . Acetyl CoA recognition is mediated by a beta alpha structure derived from GNAT motif A, which presents an invariant Arg/Gln-X-X-Gly-X-Gly/ Ala segment for hydrogen bonding with the cofactor. Motif B contribute s acidic residues to the binding site for the positively charged antib iotic substrate.