%0 Journal Article
%T Fully closed conformation of penicillin-binding protein revealed by structure of PBP2 from Acinetobacter baumannii.
%A Jang H
%A Kim CM
%A Hong E
%A Park HH
%J Biochem Biophys Res Commun
%V 729
%N 0
%D 2024 Oct 15
%M 38986258
%F 3.322
%R 10.1016/j.bbrc.2024.150368
%X Penicillin-binding protein 2 (PBP2), a vital protein involved in bacterial cell-wall synthesis, serves a target for β-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.