...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Determination of the structure of an endoglucanase from Aspergillus niger and its mode of inhibition by palladium chloride.
【24h】

Determination of the structure of an endoglucanase from Aspergillus niger and its mode of inhibition by palladium chloride.

机译：确定一个内切葡聚糖酶的结构从黑曲霉及其抑制模式氯化钯。

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 fungus Aspergillus niger is a main source of industrial cellulase. beta-1,4-Endoglucanase is the major component of cellulase from A. niger. In spite of widespread applications, little is known about the structure of this enzyme. Here, the structure of beta-1,4-endoglucanase from A. niger (EglA) was determined at 2.1 A resolution. Although there is a low sequence identity between EglA and CelB2, another member of family 12, the three-dimensional structures of their core regions are quite similar. The structural differences are mostly found in the loop regions, where CelB2 has an extra beta-sheet (beta-sheet C) at the non-reducing end of the binding cleft of the native enzyme. Incubation of EglA with PdCl(2) irreversibly inhibits the EglA activity. Structural studies of the enzyme-palladium complex show that three Pd(2+) ions bind to each EglA molecule. One of the Pd(2+) ions forms a coordinate covalent bond with Met118 S(delta) and the nucleophilic Glu116 O(epsilon1) at the active site of the enzyme. The other two Pd(2+) ions bind on the surface of the protein. Binding of Pd(2+) ions to EglA does not change the general conformation of the backbone of the protein significantly. Based on this structural study, one can conclude that the palladium ion directly binds to and blocks the active site of EglA and thus inactivates the enzyme.
机译：真菌黑曲霉的主要来源工业纤维素酶。纤维素酶的主要组件从尼日尔。尽管广泛应用,很少知道这种酶的结构。4-endoglucanase从beta 1的结构。尼日尔(EglA) 2.1决议决定。虽然有较低的序列之间的身份EglA CelB2,另一个家庭成员12日其核心的三维结构地区十分相似。差异主要是在循环区域,CelB2有一个额外的β褶板(β褶板吗C)在非还绑定裂的原生酶。PdCl(2)不可逆地抑制EglA活动。enzyme-palladium的结构的研究复杂的显示三个Pd(2 +)离子结合EglA分子。协调与Met118年代(δ)和共价键亲核Glu116 O (epsilon1)活跃的酶。结合表面的蛋白质。Pd(2 +)离子EglA不会改变蛋白质的构象的骨干显著。一个可以直接得出结论,钯离子结合EglA的活性部位和块从而使酶失去活性。

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