Abstract：
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.
摘要：
青霉素结合蛋白2（PBP2），一种参与细菌细胞壁合成的重要蛋白质，作为β-内酰胺抗生素的靶标。鲍曼不动杆菌是一种因多重耐药而臭名昭著的病原体；因此，探索PBP在开发新的抗菌策略中至关重要。在这项研究中,使用X射线晶体学阐明了鲍曼不动杆菌（abPBP2）的PBP2的三级结构。结构分析表明在头域有明显的运动，它的糖基转移酶功能可能至关重要，表明abPBP2呈现完全封闭的构象。我们的发现为开发针对abPBP2的新型抗微生物剂提供了有价值的信息，这些抗微生物剂适用于对抗多药耐药感染。
