• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >X-ray structure of Escherichia coli pyridoxine 5 '-phosphate oxidasecomplexed with pyridoxal 5 '-phosphate at 2.0 angstrom resolution
【24h】

X-ray structure of Escherichia coli pyridoxine 5 '-phosphate oxidasecomplexed with pyridoxal 5 '-phosphate at 2.0 angstrom resolution

机译：大肠杆菌吡ido醇5'-磷酸氧化酶与吡ido醛5'-磷酸复合的X射线结构，分辨率为2.0埃

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

Escherichia coil pyridoxine 5 ' -phosphate oxidase catalyzes the terminal step in the biosynthesis of pyridoxal 5 ' -phosphate by the FMN oxidation of pyridoxine 5 ' -phosphate forming FMNH2 and H2O2. Recent studies have shown that in addition to the active site, pyridoxine 5 ' -phosphate oxidase contains a non-catalytic site that binds pyridoxal 5 ' -phosphate tightly. The crystal structure of pyridoxine 5 ' -phosphate oxidase from E. coil with one or two molecules of pyridoxal 5 ' -phosphate bound to each monomer has been determined to 2.0 Angstrom resolution. One of the pyridoxal 5 ' -phosphate molecules is clearly bound at the active site with the aldehyde at C4 ' of pyridoxal 5 ' -phosphate near N5 of the bound FMN. A protein conformational change has occurred that partially closes the active site. The orientation of the bound pyridoxal 5 ' -phosphate suggests that the enzyme catalyzes a hydride ion transfer between C4 ' of pyridoxal 5 ' -phosphate and N5 of FMN. When the crystals are soaked with excess pyridoxal 5 ' -phosphate an additional molecule of this cofactor is also bound about 11 Angstrom from the active site. A possible tunnel exists between the two sites so that pyridoxal 5 ' -phosphate formed at the active site may transfer to the non-catalytic site without passing though the solvent.
机译：大肠埃希氏螺旋体吡ido醇5'-磷酸氧化酶通过吡MN醇5'-磷酸的FMN氧化形成FMNH2和H2O2催化吡ido醛5'-磷酸的生物合成中的最终步骤。最近的研究表明，除活性位点外，吡ido醇5'-磷酸氧化酶还包含一个非催化位点，它与吡ido醛5'-磷酸紧密结合。已经确定来自大肠杆菌的吡ido醇5'-磷酸氧化酶的晶体结构具有结合至每个单体的一个或两个分子吡ido醛5'-磷酸分子至2.0埃分辨率。吡ido醛5'-磷酸酯分子之一在活性位点清楚地与醛基吡咯醛5'-磷酸酯的C4'在结合的FMN的N5附近的醛结合。发生了蛋白质构象变化，部分关闭了活性位点。结合的吡ido醛5'-磷酸的取向表明该酶催化吡ido醛5'-磷酸的C4'和FMN的N5之间的氢化物离子转移。当晶体用过量的吡al醛5'-磷酸盐浸泡时，该辅因子的另一分子也与活性位点结合约11埃。在两个位点之间可能存在一个通道，因此在活性位点形成的吡ido醛5'-磷酸盐可以转移到非催化位点，而不会通过溶剂。

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