1BO4

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

Summary for 1BO4

• Entry DOI: 10.2210/pdb1bo4/pdb
• Descriptor: PROTEIN (SERRATIA MARCESCENS AMINOGLYCOSIDE-3-N-ACETYLTRANSFERASE), SPERMIDINE, COENZYME A, ... (4 entities in total)
• Functional Keywords: aminoglycoside 3-n-acetyltransferase, eubacterial aminoglycoside resistance, gcn5-related n-acetyltransferase, coa-binding, transferase
• Biological source: Serratia marcescens
• Total number of polymer chains: 2
• Total formula weight: 38656.28

Authors

Wolf, E.,Vassilev, A.,Makino, Y.,Sali, A.,Nakatani, Y.,Burley, S.K. (deposition date: 1998-08-08, release date: 1998-10-07, Last modification date: 2024-02-07)

Primary citation

Wolf, E.,Vassilev, A.,Makino, Y.,Sali, A.,Nakatani, Y.,Burley, S.K.
Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase.
Cell(Cambridge,Mass.), 94:439-449, 1998

PubMed Abstract: 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.

PubMed: 9727487
DOI: 10.1016/S0092-8674(00)81585-8

Experimental method

X-RAY DIFFRACTION (2.3 Å)