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首页> 外文期刊>Journal of bacteriology >Crystal Structure of the YgfZ Protein from Escherichia coli Suggests a Folate-Dependent Regulatory Role in One-Carbon Metabolism
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Crystal Structure of the YgfZ Protein from Escherichia coli Suggests a Folate-Dependent Regulatory Role in One-Carbon Metabolism

机译：来自大肠杆菌的YgfZ蛋白的晶体结构表明叶酸依赖于一碳代谢的调节作用。

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摘要

The ygfZ gene product of Escherichia coli represents a large protein family conserved in bacteria to eukaryotes. The members of this family are uncharacterized proteins with marginal sequence similarity to the T-protein (aminomethyltransferase) of the glycine cleavage system. To assist with the functional assignment of the YgfZ family, the crystal structure of the E. coli protein was determined by multiwavelength anomalous diffraction. The protein molecule has a three-domain architecture with a central hydrophobic channel. The structure is very similar to that of bacterial dimethylglycine oxidase, an enzyme of the glycine betaine pathway and a homolog of the T-protein. Based on structural superposition, a folate-binding site was identified in the central channel of YgfZ, and the ability of YgfZ to bind folate derivatives was confirmed experimentally. However, in contrast to dimethylglycine oxidase and T-protein, the YgfZ family lacks amino acid conservation at the folate site, which implies that YgfZ is not an aminomethyltransferase but is likely a folate-dependent regulatory protein involved in one-carbon metabolism.
机译：大肠埃希氏菌的 ygfZ 基因产物代表在细菌中对真核生物保守的一个大蛋白家族。该家族的成员是未表征的蛋白质，其边缘序列与甘氨酸切割系统的T蛋白（氨基甲基转移酶）相似。为了协助YgfZ家族的功能分配， E的晶体结构。多波长异常衍射法测定大肠杆菌蛋白。蛋白质分子具有带中央疏水通道的三结构域结构。该结构与细菌二甲基甘氨酸氧化酶，甘氨酸甜菜碱途径的酶和T蛋白的同源物非常相似。基于结构叠加，在YgfZ的中央通道中确定了叶酸结合位点，并通过实验证实了YgfZ结合叶酸衍生物的能力。但是，与二甲基甘氨酸氧化酶和T蛋白相反，YgfZ家族在叶酸位点缺乏氨基酸保守性，这意味着YgfZ不是氨基甲基转移酶，而是可能是叶酸依赖性调节蛋白，参与一碳代谢。

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