8ZPC

Acinetobacter baumannii Penicillin-Binding Protein 2

Summary for 8ZPC

• Entry DOI: 10.2210/pdb8zpc/pdb
• Descriptor: Peptidoglycan D,D-transpeptidase MrdA (1 entity in total)
• Functional Keywords: penicllin-binding protein 2, pbp2, hydrolase
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 2
• Total formula weight: 139321.38

Authors

Jang, H.S.,Park, H.H. (deposition date: 2024-05-29, release date: 2024-12-04)

Primary citation

Jang, H.,Kim, C.M.,Hong, E.,Park, H.H.
Fully closed conformation of penicillin-binding protein revealed by structure of PBP2 from Acinetobacter baumannii.
Biochem.Biophys.Res.Commun., 729:150368-150368, 2024

PubMed 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.

PubMed: 38986258
DOI: 10.1016/j.bbrc.2024.150368

Experimental method

X-RAY DIFFRACTION (3.313 Å)