Crystal structure of the YgfZ protein from Escherichia coli suggests a folate-dependent regulatory role in one-carbon metabolism.
Crystal structure of the YgfZ protein from Escherichia coli suggests a folate-dependent regulatory role in one-carbon metabolism.
复制标题
大肠杆菌 YgfZ 蛋白的晶体结构表明在一碳代谢中具有叶酸依赖性调节作用。
DOI：
10.1128/jb.186.21.7134-7140.2004
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发表时间：
2004
影响因子：
3.2
通讯作者：
Gilliland,GaryL
中科院分区：
文献类型：
--
作者：
Teplyakov,Alexey;Obmolova,Galina;Sarikaya,Elif;Pullalarevu,Sadhana;Krajewski,Wojciech;Galkin,Andrey;Howard,AndrewJ;Herzberg,Osnat;Gilliland,GaryL
大肠杆菌的gfz基因产物代表了一个在细菌到真核生物中保守的大蛋白家族。该家族的成员是与甘氨酸切割系统的t蛋白（氨基甲基转移酶）边缘序列相似的未被鉴定的蛋白质。为了协助YgfZ家族的功能分配，分析了theE的晶体结构。采用多波长异常衍射法测定大肠杆菌蛋白。该蛋白分子具有三结构域结构，具有中心疏水通道。其结构与细菌二甲基甘氨酸氧化酶非常相似，二甲基甘氨酸氧化酶是甘氨酸甜菜碱途径的一种酶，也是t蛋白的同源物。基于结构叠加，在YgfZ的中心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。然而，与二甲基甘氨酸氧化酶和t蛋白相比，YgfZ家族在叶酸位点缺乏氨基酸保护，这意味着YgfZ不是一种氨基甲基转移酶，而可能是一种参与单碳代谢的叶酸依赖性调节蛋白。
TheygfZgene product ofEscherichia colirepresents 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 theE. coliprotein 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.