Crystal structure of the tubulin tyrosine carboxypeptidase complex VASH1–SVBP
Publication date
2019-07-01
Authors
Adamopoulos, Athanassios
Landskron, Lisa
Heidebrecht, Tatjana
Tsakou, Foteini
Bleijerveld, Onno
Altelaar, A.F. Maarten
Nieuwenhuis, Joppe
Celie, Patrick H.N.
Brummelkamp, Thijn R.
Perrakis, Anastassis
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Document Type
Article
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taverne
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.
Keywords
Taverne, Structural Biology, Molecular Biology
Citation
Adamopoulos, A, Landskron, L, Heidebrecht, T, Tsakou, F, Bleijerveld, O B, Altelaar, M, Nieuwenhuis, J, Celie, P H N, Brummelkamp, T R & Perrakis, A 2019, 'Crystal structure of the tubulin tyrosine carboxypeptidase complex VASH1–SVBP', Nature Structural and Molecular Biology, vol. 26, no. 7, pp. 567-570. https://doi.org/10.1038/s41594-019-0254-6