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首页> 外文期刊>Journal of Molecular Biology >The UBX domain: A widespread ubiquitin-like module
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The UBX domain: A widespread ubiquitin-like module

机译：UBX域：广泛的泛素样模块

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摘要

The UBX domain is an 80 amino acid residue module that is present typically at the carboxyl terminus of a variety of eukaryotic proteins. In an effort to elucidate the function of UBX domains, we solved the three-dimensional structure of the UBX domain of human Fas-associated factor-1 (FAF1) by NMR spectroscopy. The structure has a P-Grasp fold characterised by a beta-beta-alpha-beta-beta-alpha-beta secondary-structure organisation. The five beta strands are arranged into a mixed sheet in the order 21534. The longer first helix packs across the first three strands of the sheet, and a second shorter 3(10) helix is located in an extended loop connecting strands 4 and 5. In the absence of significant sequence similarity, the UBX domain can be superimposed with ubiquitin with an r.m.s.d. of 1.9 Angstrom, suggesting that the true structures share the same superfold, and an evolutionary relationship. However, the absence of a carboxyl-terminal extension containing a double glycine motif and of suitably positioned lysine side-chains makes it highly unlikely that UBX domains are either conju gated to other proteins or part of mixed UBX-ubiquitin chains. Database searches revealed that most UBX domain-containing proteins belong to one of four evolutionarily consen ed families represented by the human FAF1, p47, Y33K, and Rep8 proteins. A role of the UBX domain in ubiquitin-related processes is suggested.
机译：UBX结构域是一个80个氨基酸的残基模块，通常存在于多种真核蛋白的羧基末端。为了阐明UBX域的功能，我们通过NMR光谱解析了人类Fas相关因子1（FAF1）UBX域的三维结构。该结构具有P-抓褶的特征是β-β-α-β-β-α-β二级结构组织。五个β链按21534的顺序排列成一个混合的薄片。较长的第一螺旋堆积在薄片的前三根螺旋上，第二个较短的3（10）螺旋位于一个延伸的回路中，该回路连接链4和5。在没有显着的序列相似性的情况下，UBX结构域可以与具有rmsd的泛素重叠1.9埃，表明真实结构具有相同的超折叠，并且具有进化关系。然而，由于缺乏包含双甘氨酸基序和适当位置的赖氨酸侧链的羧基末端延伸，因此极不可能将UBX结构域与其他蛋白质或部分混合的UBX-泛素链缀合。数据库搜索显示，大多数包含UBX域的蛋白质属于以人类FAF1，p47，Y33K和Rep8蛋白质为代表的四个进化同意的家族之一。建议UBX域在泛素相关过程中的作用。

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