• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8.
【24h】

Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8.

机译：嗜热栖热菌HB8的赖氨酸生物合成酶LysX的晶体结构。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The thermophilic bacterium Thermus thermophilus synthesizes lysine through the alpha-aminoadipate pathway, which uses alpha-aminoadipate as a biosynthetic intermediate of lysine. LysX is the essential enzyme in this pathway, and is believed to catalyze the acylation of alpha-aminoadipate. We have determined the crystal structures of LysX and its complex with ADP at 2.0A and 2.38A resolutions, respectively. LysX is composed of three alpha+beta domains, each composed of a four to five-stranded beta-sheet core flanked by alpha-helices. The C-terminal and central domains form an ATP-grasp fold, which is responsible for ATP binding. LysX has two flexible loop regions, which are expected to play an important role in substrate binding and protection. In spite of the low level of sequence identity, the overall fold of LysX is surprisingly similar to that of other ATP-grasp fold proteins, such as D-Ala:D-Ala ligase, PurT-encoded glycinamide ribonucleotide transformylase, glutathione synthetase, and synapsin I. In particular, they share a similar spatial arrangement of the amino acid residues around the ATP-binding site. This observation strongly suggests that LysX is an ATP-utilizing enzyme that shares a common evolutionary ancestor with other ATP-grasp fold proteins possessing a carboxylate-amine/thiol ligase activity.
机译：嗜热细菌嗜热栖热菌通过α-氨基己二酸途径合成赖氨酸，该途径使用α-氨基己二酸作为赖氨酸的生物合成中间体。 LysX是该途径中必不可少的酶，据信可催化α-氨基己二酸酯的酰化作用。我们已经分别确定了LysX的晶体结构及其与ADP的配合物的分辨率为2.0A和2.38A。 LysX由三个alpha + beta结构域组成，每个结构域均由一个4至5链的beta-sheet核心（两侧为alpha-螺旋）组成。 C末端和中央结构域形成ATP-抓握折叠，其负责ATP结合。 LysX具有两个柔性环区，预期在底物结合和保护中起重要作用。尽管序列同一性水平较低，但LysX的整体折叠却与其他ATP抓握折叠蛋白（例如D-Ala：D-Ala连接酶，PurT编码的甘氨酰胺核糖核苷酸转化酶，谷胱甘肽合成酶和特别是，它们在ATP结合位点附近具有相似的氨基酸残基空间排列。该观察结果强烈表明，LysX是一种利用ATP的酶，与其他具有羧酸盐-胺/硫醇连接酶活性的ATP抓握折叠蛋白共享共同的祖先。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号