Structure of the UBA domain of Dsk2p in complex with ubiquitin: Molecular determinants for ubiquitin recognition
Structure of the UBA domain of Dsk2p in complex with ubiquitin: Molecular determinants for ubiquitin recognition
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DOI：
10.1016/j.str.2005.01.011
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发表时间：
2005-04-01
期刊：
影响因子：
5.7
通讯作者：
Shirakawa, M
中科院分区：
文献类型：
--
作者：
Ohno, A;Jee, J;Shirakawa, M
泛素相关 (UBA) 结构域是识别泛素标签最常见的基序之一。 Dsk2p 是一种来自酿酒酵母的含有 UBA 的蛋白质，参与泛素蛋白酶体蛋白水解途径，并与纺锤体极复制有关。在这里，我们展示了 Dsk2p 的 UBA 结构域 (Dsk2(UBA)) 与泛素复合物的溶液结构。该结构表明，UBA 结构域使用与 CUE 结构域相似的泛素识别模式，CUE 结构域是另一种泛素结合基序，与 UBA 结构域具有较低的序列同源性，但具有较高的结构相似性。这两个结构域以及结构上不相关的泛素结合基序 UIM 为泛素提供了一个常见且关键的识别位点，其中包含一个 Gly-47 酰胺基的氢键受体，以及一个挤在由 Leu-8、Ile-44、His-68 和 Val-70 形成的泛素疏水口袋上的甲基。
The ubiquitin-associated (UBA) domain is one of the most frequently occurring motifs that recognize ubiquitin tags. Dsk2p, a UBA-containing protein from Saccharomyces cerevisiae, is involved in the ubiquitin-proteasome proteolytic pathway and has been implicated in spindle pole duplication. Here we present the solution structure of the UBA domain of Dsk2p (Dsk2(UBA)) in complex with ubiquitin. The structure reveals that the UBA domain uses a mode of ubiquitin recognition that is similar to that of the CUE domain, another ubiquitin binding motif that shares low sequence homology but high structural similarity with UBA domains. These two domains, as well as the structurally unrelated ubiquitin binding motif UIM, provide a common, crucial recognition site for ubiquitin, comprising a hydrogen-bonding acceptor for the amide group of Gly-47, and a methyl group that packs against the hydrophobic pocket of ubiquitin formed by Leu-8, Ile-44, His-68, and Val-70.