Solution structure and dynamics of Ufm1, a ubiquitin-fold modifier 1
Solution structure and dynamics of Ufm1, a ubiquitin-fold modifier 1
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DOI：
10.1016/j.bbrc.2006.02.107
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发表时间：
2006-04-28
影响因子：
3.1
通讯作者：
Kato, K
中科院分区：
文献类型：
--
作者：
Sasakawa, H;Sakata, E;Kato, K
泛素折叠修饰物1（Ufm 1）是多种泛素样修饰物之一，并通过Uba 5（E1）和Ufc 1（E2）与细胞中的靶蛋白缀合。Ufm 1系统在后生动物和植物中是保守的，这表明它在各种多细胞生物中具有潜在的作用。在此，我们分析了解决方案的结构和动力学的人Ufm 1（hsUfm 1）的核磁共振光谱。虽然hsUfm 1的全局折叠与泛素（Ub）和NEDD 8的相似，但Ub和NEDD 8中保守的酸性残基簇不存在于Ufm 1表面上。N-15自旋弛豫数据显示，hsUfm 1的氨基酸残基表现出构象波动，形成一个簇在C-末端片段和其空间接近，这对应于Ub和其他泛素样蛋白（Ubls）的通用配体结合位点。我们认为，Ub和其他Ubl修饰剂共享一个共同的特点，潜在的构象多样性，这可能与广泛的配体特异性，这些蛋白质。(c)2006年爱思唯尔公司All rights reserved.
The ubiquitin-fold modifier 1 (Ufm 1) is one of various ubiquitin-like modifiers and conjugates to target proteins in cells through Uba5 (E1) and Ufc1 (E2). The Ufm1-system is conserved in metazoa and plants, suggesting its potential roles in various tnulticellular organisms. Herein, we analyzed the solution structure and dynamics of human Ufm1 (hsUfm1) by nuclear magnetic resonance spectroscopy. Although the global fold of hsUfm1 is similar to those of ubiquitin (Ub) and NEDD8, the cluster of acidic residues conserved in Ub and NEDD8 does not exist on the Ufm1 surface. N-15 spin relaxation data revealed that the amino acid residues of hsUfm1 exhibiting conformational fluctuations form a cluster at the C-terminal segment and its spatial proximity, which correspond to the versatile ligand-binding sites of Ub and other ubiquitin-like proteins (Ubls). We suggest that Ub and other Ubl-modifiers share a common feature of potential conformational multiplicity, which might be associated with the broad ligand specificities of these proteins. (c) 2006 Elsevier Inc. All rights reserved.