5OE0

CRYSTAL STRUCTURE OF THE BETA-LACTAMASE OXA-181

5OE0 の概要

• エントリーDOI: 10.2210/pdb5oe0/pdb
• 分子名称: Beta-lactamase, CHLORIDE ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: antibiotic resistance, oxacillinase, oxa-48-like, carbapenemase, antibiotic
• 由来する生物種: Klebsiella pneumoniae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60918.91

構造登録者

Lund, B.A.,Carlsen, T.J.O.,Leiros, H.K.S.,Thomassen, A.M. (登録日: 2017-07-07, 公開日: 2017-08-02, 最終更新日: 2024-01-17)

主引用文献

Lund, B.A.,Thomassen, A.M.,Carlsen, T.J.O.,Leiros, H.K.S.
Structure, activity and thermostability investigations of OXA-163, OXA-181 and OXA-245 using biochemical analysis, crystal structures and differential scanning calorimetry analysis.
Acta Crystallogr F Struct Biol Commun, 73:579-587, 2017

PubMed Abstract: The first crystal structures of the class D β-lactamases OXA-181 and OXA-245 were determined to 2.05 and 2.20 Å resolution, respectively; in addition, the structure of a new crystal form of OXA-163 was resolved to 2.07 Å resolution. All of these enzymes are OXA-48-like and have been isolated from different clinical Klebsiella pneumoniae strains and also from other human pathogens such as Pseudomonas aeruginosa and Escherichia coli. Here, enzyme kinetics and thermostability studies are presented, and the new crystal structures are used to explain the observed variations. OXA-245 had the highest melting point (T = 55.8°C), as determined by differential scanning calorimetry, compared with OXA-163 (T = 49.4°C) and OXA-181 (T = 52.6°C). The differences could be explained by the loss of two salt bridges in OXA-163, and an overall decrease in the polarity of the surface of OXA-181 compared with OXA-245.

PubMed: 28994407
DOI: 10.1107/S2053230X17013838

実験手法

X-RAY DIFFRACTION (2.05000841209 Å)