3BYD
Crystal structure of beta-lactamase OXY-1-1 from Klebsiella oxytoca
Summary for 3BYD
| Entry DOI | 10.2210/pdb3byd/pdb |
| Descriptor | Beta-lactamase OXY-1, SULFATE ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | multi-domain proteins (alpha and beta), antibiotic resistance, hydrolase |
| Biological source | Klebsiella oxytoca |
| Total number of polymer chains | 1 |
| Total formula weight | 29049.66 |
| Authors | Liang, Y.-H.,Wu, S.W.,Su, X.-D. (deposition date: 2008-01-15, release date: 2009-01-20, Last modification date: 2023-11-01) |
| Primary citation | Liang, Y.-H.,Gao, R.,Su, X.-D. Structural insights into the broadened substrate profile of the extended-spectrum beta-lactamase OXY-1-1 from Klebsiella oxytoca Acta Crystallogr.,Sect.D, 68:1460-1467, 2012 Cited by PubMed Abstract: Klebsiella oxytoca is a pathogen that causes serious infections in hospital patients. It shows resistance to many clinically used β-lactam antibiotics by producing chromosomally encoded OXY-family β-lactamases. Here, the crystal structure of an OXY-family β-lactamase, OXY-1-1, determined at 1.93 Å resolution is reported. The structure shows that the OXY-1-1 β-lactamase has a typical class A β-lactamase fold and exhibits greater similarity to CTX-M-type β-lactamases than to TEM-family or SHV-family β-lactamases. It is also shown that the enzyme provides more space around the active cavity for the R(1) and R(2) substituents of β-lactam antibiotics. The half-positive/half-negative distribution of surface electrostatic potential in the substrate-binding pocket indicates the preferred properties of substrates or inhibitors of the enzyme. The results reported here provide a structural basis for the broadened substrate profile of the OXY-family β-lactamases. PubMed: 23090395DOI: 10.1107/S090744491203466X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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