Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-β-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril
Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-β-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril
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DOI：
10.1016/s0022-2836(02)01271-8
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发表时间：
2003-01-24
影响因子：
5.6
通讯作者：
Dideberg, O
中科院分区：
文献类型：
--
作者：
Garcìa-Sáez, I;Mercuri, PS;Dideberg, O
β -内酰胺酶与细菌对青霉素和相关化合物的耐药性有关。金属酶类的成员现在在许多致病菌中发现，因此具有重要的临床意义。本文报道了来自戈氏荧光杆菌（FEZ-1）的zn - β -内酰胺酶在天然和复合形式下的结构。fez - 1是一种单体酶，具有两个锌结合位点。这些结构与嗜麦芽寡养单胞菌产生的四聚体L1酶的结构进行了比较。从这个分析中，参与L1寡聚化的氨基酸被清楚地识别出来。FEZ-1蛋白的活性位点虽然在折叠上相似，但却存在显著差异。先前与功能有关的两个残基在L1或FEZ-1中不存在。锌- β -内酰胺酶的广谱底物分布源于相当宽的活性位点间隙，其中可以容纳各种对内酰胺化合物。2003爱思唯尔科学有限公司版权所有。
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-I 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 P-lactam compounds can be accommodated. (C) 2003 Elsevier Science Ltd. All rights reserved.