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Structural insights into the broadened substrate profile of the extended-spectrum β-lactamase OXY-1-1 from Klebsiella oxytoca.
- Source :
-
Acta Crystallographica: Section D (Wiley-Blackwell) . Nov2012, Vol. 68 Issue 11, p1460-1467. 8p. - Publication Year :
- 2012
-
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 R1 and R2 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09074449
- Volume :
- 68
- Issue :
- 11
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section D (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 82671993
- Full Text :
- https://doi.org/10.1107/S090744491203466X