2QZ6

First crystal structure of a psychrophile class C beta-lactamase

2QZ6 の概要

• エントリーDOI: 10.2210/pdb2qz6/pdb
• 分子名称: Beta-lactamase (2 entities in total)
• 機能のキーワード: class c beta-lactamase, psychrophile, cold adaptation, antibiotic resistance, hydrolase, periplasm
• 由来する生物種: Pseudomonas fluorescens
• 細胞内の位置: Periplasm: P85302
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38764.91

構造登録者

Michaux, C.,Massant, J.,Kerff, F.,Charlier, P.,Wouters, J. (登録日: 2007-08-16, 公開日: 2008-03-18, 最終更新日: 2023-10-25)

主引用文献

Michaux, C.,Massant, J.,Kerff, F.,Docquier, J.D.,Vandenberghe, I.,Samyn, B.,Pierrard, A.,Feller, G.,Charlier, P.,Van Beeumen, J.,Wouters, J.
Crystal structure of a cold-adapted class C beta-lactamase
Febs J., 275:1687-1697, 2008

PubMed Abstract: In this study, the crystal structure of a class C beta-lactamase from a psychrophilic organism, Pseudomonas fluorescens, has been refined to 2.2 A resolution. It is one of the few solved crystal structures of psychrophilic proteins. The structure was compared with those of homologous mesophilic enzymes and of another, modeled, psychrophilic protein. The elucidation of the 3D structure of this enzyme provides additional insights into the features involved in cold adaptation. Structure comparison of the psychrophilic and mesophilic beta-lactamases shows that electrostatics seems to play a major role in low-temperature adaptation, with a lower total number of ionic interactions for cold enzymes. The psychrophilic enzymes are also characterized by a decreased number of hydrogen bonds, a lower content of prolines, and a lower percentage of arginines in comparison with lysines. All these features make the structure more flexible so that the enzyme can behave as an efficient catalyst at low temperatures.

PubMed: 18312599
DOI: 10.1111/j.1742-4658.2008.06324.x

実験手法

X-RAY DIFFRACTION (2.26 Å)