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首页> 外文期刊>Journal of Molecular Biology >The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway
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The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway

机译：大肠杆菌MoeA的晶体结构，Modbdopterin合成途径的蛋白质

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摘要

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 Angstrom 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. (C) 2001 Academic Press. [References: 62]
机译：尽管MoeA的功能尚未明确定义，但它参与了Molybdopterin辅因子的合成。大肠杆菌蛋白质的三维结构在2.2埃分辨率下解析。原核和真核MoeA同源物中高度保守的残基的位置将二聚体界面中的裂口识别为可能的功能位点。在MoeA的四个域中，域2显示出新颖的折叠，域1和域4仅具有一个已知的结构同源物。相反，结构域3与许多其他蛋白质在结构上相似。与域3最相似的蛋白质是MogA，这是钼蝶呤辅助因子合成所需的另一种蛋白质。 MoeA和MogA之间的总体相似性以及在MoeA中高度保守的残基群中的相似性表明，这些蛋白质结合相似的配体或底物，并且可能具有相似的功能。 （C）2001学术出版社。 [参考：62]

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