• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Overexpression, crystallization and preliminary X-ray crystallographic analysis of beta-N-acetylglucosaminidase from Thermotoga maritima encoded by the Tm0809 gene
【24h】

Overexpression, crystallization and preliminary X-ray crystallographic analysis of beta-N-acetylglucosaminidase from Thermotoga maritima encoded by the Tm0809 gene

机译：Tm0809基因编码的滨海嗜热菌中β-N-乙酰氨基葡糖苷酶的过表达，结晶和初步X射线晶体学分析

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

beta-N-acetylglucosaminidase (NagA) protein hs a chitin-degrading activity and chitin is one of the most abundant polymers in nature. NagA contains a family 3 glycoside (GH3)-type N-terminal domain and a unique C-terminal domain. The structurally uncharacterized C-terminal domain of NagA may be involved in substrate specificity. To provide a structural basis for the substrate specificity of NagA, structural analysis of NagA from Thermotoga maritima encoded by the Tm0809 gene was initiated. NagA from T. maritima has been overexpressed in Escherichia coli and crystallized at 296 K using ammonium sulfate as a precipitant. Crystals of T. maritima NagA diffracted to 3.80 angstrom resolution and belonged to the monoclinic space group C2, with unit-cell parameters a = 231.15, b = 133.62, c = 140.88 angstrom, beta = 89.97 degrees. The crystallization of selenomethionyl-substituted protein is in progress to solve the crystal structure of T. maritima NagA.
机译：β-N-乙酰氨基葡萄糖苷酶（NagA）蛋白具有甲壳质降解活性，甲壳质是自然界中最丰富的聚合物之一。 NagA包含3族糖苷（GH3）型N末端域和一个独特的C末端域。 NagA的结构未表征的C末端结构域可能与底物特异性有关。为提供NagA底物特异性的结构基础，启动了由Tm0809基因编码的来自滨海嗜热菌的NagA的结构分析。来自海生螺旋杆菌的NagA已在大肠杆菌中过表达，并使用硫酸铵作为沉淀剂在296 K下结晶。海蓝藻NagA晶体衍射至3.80埃分辨率，属于单斜空间群C2，单位晶胞参数a = 231.15，b = 133.62，c = 140.88埃，β= 89.97度。硒甲硫基甲酰基取代的蛋白质的结晶正在进行中，以解决海藻T. margima NagA的晶体结构。

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