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7ONK

Crystal structure of PBP3 from P. aeruginosa in complex with AIC499

Summary for 7ONK
Entry DOI10.2210/pdb7onk/pdb
Related7ONX
DescriptorPeptidoglycan D,D-transpeptidase FtsI, (2S)-2-[(Z)-[1-(2-azanyl-1,3-thiazol-4-yl)-2-[[(2S)-3-methyl-1-oxidanylidene-3-(sulfooxyamino)butan-2-yl]amino]-2-oxidanylidene-ethylidene]amino]oxy-3-[4-[N-[(3R)-piperidin-3-yl]carbamimidoyl]phenoxy]propanoic acid, CHLORIDE ION, ... (5 entities in total)
Functional Keywordsmonobactam, pbp3, peptidoglycan synthesis, drug complex, protein binding
Biological sourcePseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Total number of polymer chains2
Total formula weight117841.15
Authors
Freischem, S.,Grimm, I.,Weiergraeber, O.H. (deposition date: 2021-05-25, release date: 2021-08-04, Last modification date: 2024-11-06)
Primary citationFreischem, 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: 34356681
DOI: 10.3390/biom11071057
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.73 Å)
Structure validation

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数据于2025-07-23公开中

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