8J40

Crystal Structure of CATB8 in complex with chloramphenicol

Summary for 8J40

• Entry DOI: 10.2210/pdb8j40/pdb
• Descriptor: CatB8, CHLORAMPHENICOL, GLYCEROL, ... (5 entities in total)
• Functional Keywords: antibiotic resistance, transferase
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 1
• Total formula weight: 26673.19

Authors

Liao, J.,Kuang, L.,Jiang, Y. (deposition date: 2023-04-18, release date: 2024-02-28, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.57 Å)