Three‐dimensional structure of the AAH26994.1 protein from Mus musculus, a putative eukaryotic Urm1
Three‐dimensional structure of the AAH26994.1 protein from Mus musculus, a putative eukaryotic Urm1
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DOI：
10.1110/ps.051577605
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发表时间：
2005-08
期刊：
影响因子：
8
通讯作者：
Shanteri Singh;M. Tonelli;R. Tyler;A. Bahrami;Min S. Lee;J. Markley
中科院分区：
文献类型：
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作者：
Shanteri Singh;M. Tonelli;R. Tyler;A. Bahrami;Min S. Lee;J. Markley
我们使用NMR光谱来确定来自小家鼠的蛋白质AAH26994.1的溶液结构，并提出它代表了泛素相关修饰物1（Urm 1）蛋白的第一个三维结构。氨基酸序列比较表明，AAH26994.1属于泛素样修饰蛋白的Urm 1家族。该家族最具特征的成员已被证明参与营养感测，侵入性生长和酵母中的出芽。该家族中的蛋白质仅与泛素具有弱的序列相似性，并且AAH26994.1的结构显示出与异蝶呤脱氢酶的MoaD亚基更接近的相似性（已知结构是与AAH26994.1具有14%-26%序列同一性的三种细菌MoaD蛋白）。AAH26994.1和MoaD蛋白的结构各自含有特征性泛素二级结构折叠，但都在该折叠之外的区域与泛素有很大不同。这种结构相似性支持了泛素和泛素相关蛋白质是从一个基于蛋白质的硫醚供体系统的多巴胺合成酶类型进化而来的假设。
We have used NMR spectroscopy to determine the solution structure of protein AAH26994.1 from Mus musculus and propose that it represents the first three‐dimensional structure of a ubiquitin‐related modifier 1 (Urm1) protein. Amino acid sequence comparisons indicate that AAH26994.1 belongs to the Urm1 family of ubiquitin‐like modifier proteins. The best characterized member of this family has been shown to be involved in nutrient sensing, invasive growth, and budding in yeast. Proteins in this family have only a weak sequence similarity to ubiquitin, and the structure of AAH26994.1 showed a much closer resemblance to MoaD subunits of molybdopterin synthases (known structures are of three bacterial MoaD proteins with 14%–26% sequence identity to AAH26994.1). The structures of AAH26994.1 and the MoaD proteins each contain the signature ubiquitin secondary structure fold, but all differ from ubiquitin largely in regions outside of this fold. This structural similarity bolsters the hypothesis that ubiquitin and ubiquitin‐related proteins evolved from a protein‐based sulfide donor system of the molybdopterin synthase type.