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-Structure paper
Title | Mutagenesis and structural analysis reveal the CTX-M beta-lactamase active site is optimized for cephalosporin catalysis and drug resistance. |
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Journal, issue, pages | J. Biol. Chem., Vol. 299, Page 104630-104630, Year 2023 |
Publish date | Jul 12, 2022 (structure data deposition date) |
Authors | Lu, S. / Montoya, M. / Hu, L. / Neetu, N. / Sankaran, B. / Prasad, B.V.V. / Palzkill, T. |
External links | J. Biol. Chem. / PubMed:36963495 |
Methods | X-ray diffraction |
Resolution | 1.36 - 1.67 Å |
Structure data | PDB-8dod: PDB-8doe: PDB-8don: PDB-8dp4: PDB-8dpq: PDB-8ela: PDB-8elb: |
Chemicals | ChemComp-K: ChemComp-HOH: ChemComp-PO4: ChemComp-EDO: ChemComp-MES: ChemComp-SO4: ChemComp-ZN: ChemComp-CL: ChemComp-PEG: |
Source |
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Keywords | HYDROLASE / Beta-lactamase / CTX-M-14 / mutation / B-lactam / antibiotic resistance / b-lactam antibiotic resistance / Beta-lactam / beta-lactamase antibiotic beta-lactam / beta-lactamase hydrolase antibiotic beta-lactam |