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微管酪氨酸羧肽酶复合物 VASH1-SVBP 的晶体结构。

Crystal structure of the tubulin tyrosine carboxypeptidase complex VASH1-SVBP.

机构信息

Division of Biochemistry, the Netherlands Cancer Institute, Amsterdam, the Netherlands.

Oncode Institute, Division of Biochemistry, the Netherlands Cancer Institute, Amsterdam, the Netherlands.

出版信息

Nat Struct Mol Biol. 2019 Jul;26(7):567-570. doi: 10.1038/s41594-019-0254-6. Epub 2019 Jul 1.

Abstract

The cyclic enzymatic removal and ligation of the C-terminal tyrosine of α-tubulin generates heterogeneous microtubules and affects their functions. Here we describe the crystal and solution structure of the tubulin carboxypeptidase complex between vasohibin (VASH1) and small vasohibin-binding protein (SVBP), which folds in a long helix, which stabilizes the VASH1 catalytic domain. This structure, combined with molecular docking and mutagenesis experiments, reveals which residues are responsible for recognition and cleavage of the tubulin C-terminal tyrosine.

摘要

环状酶促去除和连接α-微管蛋白 C 末端的酪氨酸会产生异构微管,并影响其功能。在这里,我们描述了血管抑素 (VASH1) 和小血管抑素结合蛋白 (SVBP) 之间的微管蛋白羧肽酶复合物的晶体和溶液结构,该结构折叠成长螺旋,稳定了 VASH1 的催化结构域。该结构与分子对接和突变实验相结合,揭示了哪些残基负责识别和切割微管蛋白 C 末端的酪氨酸。

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