8J40

Crystal Structure of CATB8 in complex with chloramphenicol

8J40 の概要

• エントリーDOI: 10.2210/pdb8j40/pdb
• 分子名称: CatB8, CHLORAMPHENICOL, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: antibiotic resistance, transferase
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26673.19

構造登録者

Liao, J.,Kuang, L.,Jiang, Y. (登録日: 2023-04-18, 公開日: 2024-02-28, 最終更新日: 2024-03-20)

主引用文献

Liao, J.,Qi, Q.,Kuang, L.,Zhou, Y.,Xiao, Q.,Liu, T.,Wang, X.,Guo, L.,Jiang, Y.
Chloramphenicol Binding Sites of Acinetobacter baumannii Chloramphenicol Acetyltransferase CatB8.
Acs Infect Dis., 10:870-878, 2024

PubMed Abstract: is a multidrug-resistant pathogen that has become one of the most challenging pathogens in global healthcare. Several antibiotic-resistant genes, including , have been identified in the genome. CatB8 protein, one of the chloramphenicol acetyltransferases (Cats), is encoded by the gene. Cats can convert chloramphenicol (chl) to 3-acetyl-chl, leading to bacterial resistance to chl. Here, we present the high-resolution cocrystal structure of CatB8 with chl. The structure that we resolved showed that each monomer of CatB8 binds to four chl molecules, while its homologous protein only binds to one chl molecule. One of the newly discovered chl binding site overlaps with the site of another substrate, acetyl-CoA. Through structure-based biochemical analyses, we identified key residues for chl recruiting and acetylation of chl in CatB8. Our work is of significant importance for understanding the drug resistance of and the effectiveness of antibiotic treatment.

PubMed: 38311919
DOI: 10.1021/acsinfecdis.3c00359

実験手法

X-RAY DIFFRACTION (1.57 Å)