Structural highlights
Function
G1C6X4_ACIBA Catalyzes cross-linking of the peptidoglycan cell wall.[HAMAP-Rule:MF_02081]
Publication Abstract from PubMed
Penicillin-binding protein 2 (PBP2), a vital protein involved in bacterial cell-wall synthesis, serves a target for beta-lactam antibiotics. Acinetobacter baumannii is a pathogen notorious for multidrug resistance; therefore, exploration of PBPs is pivotal in the development of new antimicrobial strategies. In this study, the tertiary structure of PBP2 from A. baumannii (abPBP2) was elucidated using X-ray crystallography. The structural analysis demonstrated notable movement in the head domain, potentially critical for its glycosyltransferase function, suggesting that abPBP2 assumes a fully closed conformation. Our findings offer valuable information for developing novel antimicrobial agents targeting abPBP2 that are applicable in combating multidrug-resistant infections.
Fully closed conformation of penicillin-binding protein revealed by structure of PBP2 from Acinetobacter baumannii.,Jang H, Kim CM, Hong E, Park HH Biochem Biophys Res Commun. 2024 Oct 15;729:150368. doi: , 10.1016/j.bbrc.2024.150368. Epub 2024 Jul 6. PMID:38986258[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jang H, Kim CM, Hong E, Park HH. Fully closed conformation of penicillin-binding protein revealed by structure of PBP2 from Acinetobacter baumannii. Biochem Biophys Res Commun. 2024 Oct 15;729:150368. PMID:38986258 doi:10.1016/j.bbrc.2024.150368
