4YIN
Crystal structure of the extended-spectrum beta-lactamase OXA-145
Summary for 4YIN
| Entry DOI | 10.2210/pdb4yin/pdb |
| Descriptor | Beta-lactamase, CITRATE ANION (3 entities in total) |
| Functional Keywords | antibiotic resistance, extended-spectrum beta-lactamase, class d, oxacillinase, hydrolase |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 2 |
| Total formula weight | 55106.45 |
| Authors | Meziane-Cherif, D.,Bonnet, R.,Haouz, A.,Courvalin, P. (deposition date: 2015-03-02, release date: 2016-02-10, Last modification date: 2024-10-23) |
| Primary citation | Meziane-Cherif, D.,Bonnet, R.,Haouz, A.,Courvalin, P. Structural insights into the loss of penicillinase and the gain of ceftazidimase activities by OXA-145 beta-lactamase in Pseudomonas aeruginosa. J. Antimicrob. Chemother., 71:395-402, 2016 Cited by PubMed Abstract: We previously described extended-spectrum oxacillinase OXA-145 from Pseudomonas aeruginosa, which differs from narrow-spectrum OXA-35 by loss of Leu-155. The deletion results in loss of benzylpenicillin hydrolysis and acquisition of activity against ceftazidime. We report the crystal structure of OXA-145 and provide the basis of its switch in substrate specificity. PubMed: 26568564DOI: 10.1093/jac/dkv375 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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