From the first to the second domain of gelsolin: a common path on the surface of actin?
From the first to the second domain of gelsolin: a common path on the surface of actin?
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DOI：
10.1016/s0014-5793(03)00934-7
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发表时间：
2003-09-25
期刊：
影响因子：
3.5
通讯作者：
Robinson, RC
中科院分区：
文献类型：
--
作者：
Irobi, E;Burtnick, LD;Robinson, RC
我们介绍了2.6。G-actin和凝溶胶蛋白片段Met 25-GIn 160（G1+）之间形成的复合物的解析晶体结构。其结构不同于其他凝溶胶蛋白结构域1（G1）复合物，因为从关键的连接区到凝溶胶蛋白结构域2（G2）的另外6个氨基酸残基是可见的，并且牢固地附着在肌动蛋白表面。连接片段从G1延伸到肌动蛋白的表面，其方向推断G2将沿着与肌动蛋白结合到G1的相同长螺距螺旋链沿着结合。这与G2将凝溶胶蛋白附着在细丝的一侧，然后将G1引导到它将破坏肌动蛋白-肌动蛋白接触的位置的机制一致。G1-G2接头内结构上重要的残基序列与WH 2（WASp同源结构域2）结构域蛋白家族成员（例如WASp（Wiscott-Aldridge综合征蛋白）和胸腺素β 4）的序列比对表明，细丝组装和拆卸的相反活性可能利用了肌动蛋白表面上的共同补丁。(C)2003年由Elsevier B. V.代表欧洲生物化学学会联合会出版。
We present the 2.6. resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25-GIn160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin-actin contacts. Alignment of the sequence of the structurally important residues within the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin beta4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.