3BYD

Crystal structure of beta-lactamase OXY-1-1 from Klebsiella oxytoca

3BYD の概要

• エントリーDOI: 10.2210/pdb3byd/pdb
• 分子名称: Beta-lactamase OXY-1, SULFATE ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: multi-domain proteins (alpha and beta), antibiotic resistance, hydrolase
• 由来する生物種: Klebsiella oxytoca
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29049.66

構造登録者

Liang, Y.-H.,Wu, S.W.,Su, X.-D. (登録日: 2008-01-15, 公開日: 2009-01-20, 最終更新日: 2023-11-01)

主引用文献

Liang, Y.-H.,Gao, R.,Su, X.-D.
Structural insights into the broadened substrate profile of the extended-spectrum beta-lactamase OXY-1-1 from Klebsiella oxytoca
Acta Crystallogr.,Sect.D, 68:1460-1467, 2012

PubMed Abstract: Klebsiella oxytoca is a pathogen that causes serious infections in hospital patients. It shows resistance to many clinically used β-lactam antibiotics by producing chromosomally encoded OXY-family β-lactamases. Here, the crystal structure of an OXY-family β-lactamase, OXY-1-1, determined at 1.93 Å resolution is reported. The structure shows that the OXY-1-1 β-lactamase has a typical class A β-lactamase fold and exhibits greater similarity to CTX-M-type β-lactamases than to TEM-family or SHV-family β-lactamases. It is also shown that the enzyme provides more space around the active cavity for the R(1) and R(2) substituents of β-lactam antibiotics. The half-positive/half-negative distribution of surface electrostatic potential in the substrate-binding pocket indicates the preferred properties of substrates or inhibitors of the enzyme. The results reported here provide a structural basis for the broadened substrate profile of the OXY-family β-lactamases.

PubMed: 23090395
DOI: 10.1107/S090744491203466X

実験手法

X-RAY DIFFRACTION (1.93 Å)