7ONZ
Crystal structure of PBP3 from P. aeruginosa
Summary for 7ONZ
Entry DOI | 10.2210/pdb7onz/pdb |
Related | 7ONX |
Descriptor | Peptidoglycan D,D-transpeptidase FtsI, GLYCEROL (3 entities in total) |
Functional Keywords | pbp3, peptidoglycan synthesis, membrane protein |
Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
Total number of polymer chains | 1 |
Total formula weight | 57799.99 |
Authors | Freischem, S.,Grimm, I.,Weiergraeber, O.H. (deposition date: 2021-05-26, release date: 2021-08-04, Last modification date: 2024-01-31) |
Primary citation | Freischem, S.,Grimm, I.,Lopez-Perez, A.,Willbold, D.,Klenke, B.,Vuong, C.,Dingley, A.J.,Weiergraber, O.H. Interaction Mode of the Novel Monobactam AIC499 Targeting Penicillin Binding Protein 3 of Gram-Negative Bacteria. Biomolecules, 11:-, 2021 Cited by PubMed Abstract: Novel antimicrobial strategies are urgently required because of the rising threat of multi drug resistant bacterial strains and the infections caused by them. Among the available target structures, the so-called penicillin binding proteins are of particular interest, owing to their good accessibility in the periplasmic space, and the lack of homologous proteins in humans, reducing the risk of side effects of potential drugs. In this report, we focus on the interaction of the innovative β-lactam antibiotic AIC499 with penicillin binding protein 3 (PBP3) from and . This recently developed monobactam displays broad antimicrobial activity, against Gram-negative strains, and improved resistance to most classes of β-lactamases. By analyzing crystal structures of the respective complexes, we were able to explore the binding mode of AIC499 to its target proteins. In addition, the apo structures determined for PBP3, from and the catalytic transpeptidase domain of the orthologue, provide new insights into the dynamics of these proteins and the impact of drug binding. PubMed: 34356681DOI: 10.3390/biom11071057 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
Download full validation report
