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首页> 外文期刊>Molecular cell >The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance.
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The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance.

机译：VanX的结构揭示了一种新的氨基二肽酶，参与介导基于转座子的万古霉素耐药性。

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摘要

VanX is a zinc-dependent D-alanyl-D-alanine dipeptidase that is a critical component in a system that mediates transposon-based vancomycin resistance in enterococci. It is also a key drug target in circumventing clinical vancomycin resistance. The structure of VanX from E. faecium has been solved by X-ray crystallography and reveals a Zn(2+)-dipeptidase with a unique overall fold and a well-defined active site confined within a cavity of limited size. The crystal structures of VanX, the VanX:D-alanyl-D-alanine complex, the VanX:D-alanine complex, and VanX in complex with phosphonate and phosphinate transition-state analog inhibitors, are also presented at high resolution. Structural homology searches of known structures revealed that the fold of VanX is similar to those of two proteins: the N-terminal fragment of murine Sonic hedgehog and the Zn(2+)-dependent N-acyl-D-alanyl-D-alanine carboxypeptidase of S. albus G.
机译：VanX是锌依赖性D-丙氨酰-D-丙氨酸二肽酶，是介导肠球菌中基于转座子的万古霉素耐药性的系统中的关键组成部分。它也是规避临床万古霉素耐药性的关键药物靶标。粪肠球菌的VanX的结构已通过X射线晶体学解决，并揭示了具有独特的整体折叠和限定在有限大小的空腔内的明确定义的活性位点的Zn（2 +）-二肽酶。还以高分辨率显示了VanX，VanX：D-丙氨酰-D-丙氨酸复合物，VanX：D-丙氨酸复合物和VanX与膦酸酯和次膦酸酯过渡态类似物抑制剂形成复合物的晶体结构。对已知结构的结构同源性搜索显示，VanX的折叠与两种蛋白质的折叠相似：鼠类Sonic刺猬的N末端片段和Zn（2+）依赖的N-酰基-D-丙氨酰基-D-丙氨酸羧肽酶S. albus G.

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