5CHJ

CRYSTAL STRUCTURE OF Fox-4 cephamycinase complexed with cephalothin BATSI (SM23)

5CHJ の概要

• エントリーDOI: 10.2210/pdb5chj/pdb
• 関連するPDBエントリー: 5CGS 5CGW 5CGX 5CHM
• 分子名称: Beta-lactamase, (1R)-1-(2-THIENYLACETYLAMINO)-1-(3-CARBOXYPHENYL)METHYLBORONIC ACID, ZINC ION, ... (5 entities in total)
• 機能のキーワード: beta-lactamase, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79203.19

構造登録者

Malashkevich, V.N.,Toro, R.,Lefurgy, S.,Almo, S.C. (登録日: 2015-07-10, 公開日: 2016-08-03, 最終更新日: 2024-10-16)

主引用文献

Lefurgy, S.T.,Caselli, E.,Taracila, M.A.,Malashkevich, V.N.,Biju, B.,Papp-Wallace, K.M.,Bonanno, J.B.,Prati, F.,Almo, S.C.,Bonomo, R.A.
Structures of FOX-4 Cephamycinase in Complex with Transition-State Analog Inhibitors.
Biomolecules, 10:-, 2020

PubMed Abstract: Boronic acid transition-state analog inhibitors (BATSIs) are partners with β-lactam antibiotics for the treatment of complex bacterial infections. Herein, microbiological, biochemical, and structural findings on four BATSIs with the FOX-4 cephamycinase, a class C β-lactamase that rapidly hydrolyzes cefoxitin, are revealed. FOX-4 is an extended-spectrum class C cephalosporinase that demonstrates conformational flexibility when complexed with certain ligands. Like other β-lactamases of this class, studies on FOX-4 reveal important insights into structure-activity relationships. We show that SM23, a BATSI, shows both remarkable flexibility and affinity, binding similarly to other β-lactamases, yet retaining an IC value < 0.1 μM. Our analyses open up new opportunities for the design of novel transition-state analogs of class C enzymes.

PubMed: 32349291
DOI: 10.3390/biom10050671

実験手法

X-RAY DIFFRACTION (1.358 Å)