The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway.

The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway.
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大肠杆菌 MoeA 的晶体结构,一种来自钼蝶呤合成途径的蛋白质。

DOI:
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发表时间:
2001
影响因子:
5.6
通讯作者:
Miroslaw Cygler
Miroslaw Cygler
中科院分区:
生物学2区
文献类型:
--
作者:
J. Schrag;Weijun Huang;J. Sivaraman;Christopher R. Smith;J. Plamondon;R. Larocque;A. Matte;Miroslaw Cygler

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MOEA参与了钼掺杂蛋白辅因子的合成,但其功能尚未明确。在2.2A分辨率下对大肠杆菌蛋白的三维结构进行了解析。原核和真核MOEA同源物中高度保守的残基的位置表明,二聚体界面上的裂隙是可能的功能位点。在MOEA的四个结构域中,结构域2显示了一个新的折叠,结构域1和4分别只有一个已知的结构同源。相反,结构域3在结构上与许多其他蛋白质相似。与结构域3最相似的蛋白质是mogA,这是合成钼杂蛋白辅因子所需的另一种蛋白质。MOEA和MOGA之间的总体相似性,以及MOEA中高度保守的一系列残基的相似性,表明这些蛋白质与类似的配体或底物结合,可能具有相似的功能。
MoeA is involved in synthesis of the molybdopterin cofactor, although its function is not yet clearly defined. The three-dimensional structure of the Escherichia coli protein was solved at 2.2 A resolution. The locations of highly conserved residues among the prokaryotic and eukaryotic MoeA homologs identifies a cleft in the dimer interface as the likely functional site. Of the four domains of MoeA, domain 2 displays a novel fold and domains 1 and 4 each have only one known structural homolog. Domain 3, in contrast, is structurally similar to many other proteins. The protein that resembles domain 3 most closely is MogA, another protein required for molybdopterin cofactor synthesis. The overall similarity between MoeA and MogA, and the similarities in a constellation of residues that are strongly conserved in MoeA, suggests that these proteins bind similar ligands or substrates and may have similar functions.
DOI: 10.1126/science.284.5417.1161
发表时间: 1999-05-14
期刊: SCIENCE
影响因子: 56.9
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发表时间: 1991
期刊: The Journal of biological chemistry
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发表时间: 1995-10
影响因子: 5.6
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