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首页> 外文期刊>Journal of Molecular Biology >Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril.
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Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril.

机译：FEZ-1的三维结构，其为天然形式并与D-卡托普利复合而成的戈壁萤光菌的单体亚类B3金属β-内酰胺酶。

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摘要

The beta-lactamases are involved in bacterial resistance to penicillin and related compounds. Members of the metallo-enzyme class are now found in many pathogenic bacteria and are thus becoming of major clinical importance. The structures of the Zn-beta-lactamase from Fluoribacter gormanii (FEZ-1) in the native and in the complex form are reported here. FEZ-1 is a monomeric enzyme, which possesses two zinc-binding sites. These structures are discussed in comparison with those of the tetrameric L1 enzyme produced by Stenotrophomonas maltophilia. From this analysis, amino acids involved in the oligomerization of L1 are clearly identified. Despite the similarity in fold, the active site of FEZ-1 was found to be significantly different. Two residues, which were previously implicated in function, are not present in L1 or in FEZ-1. The broad-spectrum substrate profile of Zn-beta-lactamases arises from the rather wide active-site cleft, where various beta-lactam compounds can be accommodated.
机译：β-内酰胺酶与细菌对青霉素和相关化合物的抗性有关。现在在许多致病细菌中发现了金属酶类的成员，因此正变得具有重要的临床意义。此处报道了天然和复杂形式的戈氏萤细菌（FEZ-1）中的Zn-β-内酰胺酶的结构。 FEZ-1是一种单体酶，具有两个锌结合位点。与嗜麦芽窄食单胞菌产生的四聚体L1酶的结构相比，讨论了这些结构。通过该分析，可以清楚地识别出与L1的低聚有关的氨基酸。尽管折叠相似，但发现FEZ-1的活性位点显着不同。 L1或FEZ-1中不存在以前与功能有关的两个残基。 Zn-β-内酰胺酶的广谱底物谱来自相当宽的活性位点裂口，可以容纳各种β-内酰胺化合物。

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