1BO4

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

1BO4 の概要

• エントリーDOI: 10.2210/pdb1bo4/pdb
• 分子名称: PROTEIN (SERRATIA MARCESCENS AMINOGLYCOSIDE-3-N-ACETYLTRANSFERASE), SPERMIDINE, COENZYME A, ... (4 entities in total)
• 機能のキーワード: aminoglycoside 3-n-acetyltransferase, eubacterial aminoglycoside resistance, gcn5-related n-acetyltransferase, coa-binding, transferase
• 由来する生物種: Serratia marcescens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38656.28

構造登録者

Wolf, E.,Vassilev, A.,Makino, Y.,Sali, A.,Nakatani, Y.,Burley, S.K. (登録日: 1998-08-08, 公開日: 1998-10-07, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)