1bo4
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CRYSTAL STRUCTURE OF A GCN5-RELATED N-ACETYLTRANSFERASE: SERRATIA MARESCENS AMINOGLYCOSIDE 3-N-ACETYLTRANSFERASE
OverviewOverview
The X-ray structure of a canonical GCN5-related N-acetyltransferase, (GNAT), Serratia marcescens aminoglycoside 3-N-acetyltransferase, bound to, coenzyme A (CoA) has been determined at 2.3 A resolution. The single, domain alpha/beta protein resembles a cupped right hand wrapped around a, cylinder and consists of a highly curved, six-stranded beta sheet of mixed, polarity that is sandwiched between four alpha helices. 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 betaalpha 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 contributes acidic residues to, the binding site for the positively charged antibiotic substrate.
About this StructureAbout this Structure
1BO4 is a Single protein structure of sequence from Serratia marcescens with SPD and COA as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase., Wolf E, Vassilev A, Makino Y, Sali A, Nakatani Y, Burley SK, Cell. 1998 Aug 21;94(4):439-49. PMID:9727487
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