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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural insights into the broadened substrate profile of the extended-spectrum Β-lactamase OXY-1-1 from Klebsiella oxytoca
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Structural insights into the broadened substrate profile of the extended-spectrum Β-lactamase OXY-1-1 from Klebsiella oxytoca

机译：结构洞察扩大底物的extended-spectrumΒ内酰胺酶从克雷伯氏菌OXY-1-1 oxytoca

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摘要

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 ? 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.
机译：克雷伯氏菌oxytoca病原体引起严重的感染在医院的病人。许多临床使用阻力Β内酰胺抗生素通过产生染色体编码OXY-familyΒ-lactamases。结构的OXY-familyΒ内酰胺酶、OXY-1-1确定在1.93吗?结构表明,OXY-1-1Β内酰胺酶一个典型的a类Β内酰胺酶折叠和展览更大的相似性CTX-M-typeΒ-lactamases比TEM-family或SHV-familyΒ-lactamases。也表明,这种酶提供了更多的空间在主动腔R 1和2取代基的Β内酰胺抗生素。half-positive / half-negative分布表面静电势substrate-binding口袋里表明的首选底物或抑制剂的性质酶。扩大底物结构基础的OXY-familyΒ-lactamases。

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