Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu
Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu
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DOI：
10.1016/s0022-2836(03)00308-5
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发表时间：
2003-04-25
影响因子：
5.6
通讯作者：
Hasnain, SS
中科院分区：
文献类型：
--
作者：
Ellis, MJ;Dodd, FE;Hasnain, SS
我们提供了铜蛋白、亚硝酸还原酶和催化重要的 Asp92 残基 (D92E) 突变体的第一个原子分辨率（< 1.20 埃）结构。肽的碳-碳键清晰解析的原子分辨率仍然是结构分析的一个关键目标。尽管付出了巨大的努力和技术进步，但在这种分辨率下已知的结构仍然很少。例如，在蛋白质数据库 (PDB) 中，有大约 200 个铜蛋白结构，但分辨率最高的结构是阿米青蛋白，一种小型 (12 kDa) 蛋白质，已分辨率为 1.30 埃。在这里，我们分别以 1.04、1.15 和 1.12 埃的分辨率展示了来自木糖氧化产碱菌（36.5 kDa 单体）的野生型亚硝酸铜还原酶 (wtNiR)、“半 apo”重组天然蛋白和 D92E 突变体的结构。这些结构为构建这种重要酶的详细机制提供了基础。 (C) 2003 Elsevier Science Ltd. 保留所有权利。
We provide the first atomic resolution (< 1.20 Angstrom) structure of a copper protein, nitrite reductase, and of a mutant of the catalytically important Asp92 residue (D92E). The atomic resolution where carbon-carbon bonds of the peptide become clearly resolved, remains a key goal of structural analysis. Despite much effort and technological progress, still very few structures are known at such resolution. For example, in the Protein Data Bank (PDB) there are some 200 structures of copper proteins but the highest resolution structure is that of amicyanin, a small (12 kDa) protein, which has been resolved to 1.30 Angstrom. Here, we present the structures of wild-type copper nitrite reductase (wtNiR) from Alcaligenes xylosoxidans (36.5 kDa monomer), the "half-apo" recombinant native protein and the D92E mutant at 1.04, 1.15 and 1.12 Angstrom resolutions, respectively. These structures provide the basis from which to build a detailed mechanism of this important enzyme. (C) 2003 Elsevier Science Ltd. All rights reserved.