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Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p.泛素相关蛋白Urm1p与抗氧化蛋白Ahp1p的附着。
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Urmylation: a ubiquitin-like pathway that functions during invasive growth and budding in yeast.泛素样修饰：一种在酵母侵入性生长和出芽过程中发挥作用的类泛素途径。
Mol Biol Cell. 2003 Nov;14(11):4329-41. doi: 10.1091/mbc.e03-02-0079. Epub 2003 Jul 25.
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Project management system for structural and functional proteomics: Sesame.用于结构和功能蛋白质组学的项目管理系统：芝麻
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Structural studies of molybdopterin synthase provide insights into its catalytic mechanism.钼蝶呤合酶的结构研究为其催化机制提供了见解。
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Solution structure of ThiS and implications for the evolutionary roots of ubiquitin.硫胺素合成酶（ThiS）的溶液结构及其对泛素进化根源的启示
Nat Struct Biol. 2001 Jan;8(1):47-51. doi: 10.1038/83041.

小家鼠AAH26994.1蛋白的三维结构，一种假定的真核泛素相关修饰分子1（Urm1）

Three-dimensional structure of the AAH26994.1 protein from Mus musculus, a putative eukaryotic Urm1.

作者信息

Singh Shanteri, Tonelli Marco, Tyler Robert C, Bahrami Arash, Lee Min S, Markley John L

机构信息

Center for Eukaryotic Structural Genomics, Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706-1544, USA.

出版信息

Protein Sci. 2005 Aug;14(8):2095-102. doi: 10.1110/ps.051577605.

DOI:10.1110/ps.051577605
PMID:16046629
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2279321/
Abstract

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.

摘要

我们利用核磁共振光谱法测定了小家鼠蛋白质AAH26994.1的溶液结构，并提出它代表了泛素相关修饰因子1（Urm1）蛋白的首个三维结构。氨基酸序列比较表明，AAH26994.1属于泛素样修饰蛋白的Urm1家族。该家族中特征最明确的成员已被证明参与酵母中的营养感知、侵袭性生长和出芽过程。该家族中的蛋白质与泛素只有微弱的序列相似性，而AAH26994.1的结构与钼蝶呤合酶的MoaD亚基更为相似（已知结构的三种细菌MoaD蛋白与AAH26994.1的序列同一性为14%-26%）。AAH26994.1和MoaD蛋白的结构均包含标志性的泛素二级结构折叠，但在该折叠之外的区域与泛素大多不同。这种结构相似性支持了泛素和泛素相关蛋白从钼蝶呤合酶类型的基于蛋白质的硫化物供体系统进化而来的假说。