• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein.
【24h】

NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein.

机译：hPar14的NMR溶液结构显示出与有丝分裂调节剂hPin1的肽基脯氨酰顺/反异构酶结构域相似，但表明该蛋白的功能不同。

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 131-amino acid residue parvulin-like human peptidyl-prolyl cis/trans isomerase (PPIase) hPar14 was shown to exhibit sequence similarity to the regulator enzyme for cell cycle transitions human hPin1, but specificity for catalyzing pSer(Thr)-Pro cis/trans isomerizations was lacking. To determine the solution structure of hPar14 the (1)H, (13)C, and (15)N chemical shifts of this protein have been assigned using heteronuclear two and three-dimensional NMR experiments on unlabeled and uniformly (15)N/(13)C-labeled recombinant protein isolated from Escherichia coli cells that overexpress the protein. The chemical shift assignments were used to interpret the NOE data, which resulted in a total of 1042 NOE restraints. The NOE restraints were used along with 71 dihedral angle restraints and 38 hydrogen bonding restraints to produce 50 low-energy structures. The hPar14 folds into a betaalpha(3)betaalphabeta(2) structure, and contains an unstructured 35-amino acid basic tail N-terminal to the catalytic core that replaces the WW domain of hPin1 homologs. The three-dimensional structures of hPar14 and the PPIase domain of human hPin1 reveal a high degree of conservation. The root-mean-square deviations of the mean atomic coordinates of the heavy atoms of the backbone between residues 38 to 45, 50 to 58, 64 to 70, 81 to 86, 115 to 119 and 122 to 128 of hPar14 were 0.81(+/-0.07) A. The hPar14 model structure provides insight into how this class of PPIases may select preferential secondary catalytic sites, and also allows identification of a putative DNA-binding motif in parvulin-like PPIases. Copyright 2000 Academic Press.
机译：已显示131个氨基酸残基的小白蛋白样人肽基脯氨酰顺式/反式异构酶（PPIase）hPar14与调控酶的序列相似，可用于人hPin1的细胞周期转变，但对催化pSer（Thr）-Pro cis /缺乏反式异构化。为了确定hPar14的溶液结构，已使用杂核二维和三维NMR实验在未标记且均一的（15）N /（上）指定了该蛋白质的（1）H，（13）C和（15）N化学位移。 13）从过量表达该蛋白的大肠杆菌细胞中分离出的C标记重组蛋白。化学位移分配用于解释NOE数据，总共产生1042个NOE约束。将NOE约束与71个二面角约束和38个氢键约束一起使用可产生50个低能结构。 hPar14折叠成一个betaalpha（3）betaalphabeta（2）结构，并包含一个非结构化的35氨基酸碱性尾巴N末端的催化核心替换hPin1同源的WW域。 hPar14的三维结构和人类hPin1的PPIase结构域显示出高度的保守性。 hPar14残基38至45、50至58、64至70、81至86、115至119和122至128之间的主链重原子平均原子坐标的均方根偏差为0.81（+ /-0.07）A. hPar14模型结构提供了关于这类PPIase如何选择优先的次级催化位点的见解，并且还允许鉴定小白蛋白样PPIase中假定的DNA结合基序。版权所有2000学术出版社。

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