Crystal structure of the tubulin tyrosine carboxypeptidase complex VASH1-SVBP

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

Athanassios Adamopoulos ¹ ², Lisa Landskron ¹ ², Tatjana Heidebrecht ¹ ², Foteini Tsakou ¹, Onno B Bleijerveld ³, Maarten Altelaar ³ ⁴, Joppe Nieuwenhuis ¹ ², Patrick H N Celie ¹, Thijn R Brummelkamp ¹ ² ⁵ ⁶, Anastassis Perrakis ⁷ ⁸

Affiliations

1 Division of Biochemistry, the Netherlands Cancer Institute, Amsterdam, the Netherlands.
2 Oncode Institute, Division of Biochemistry, the Netherlands Cancer Institute, Amsterdam, the Netherlands.
3 Proteomics Facility, the Netherlands Cancer Institute, Amsterdam, the Netherlands.
4 Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands.
5 CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Vienna, Austria.
6 Cancer Genomics Center, Amsterdam, the Netherlands.
7 Division of Biochemistry, the Netherlands Cancer Institute, Amsterdam, the Netherlands. a.perrakis@nki.nl.
8 Oncode Institute, Division of Biochemistry, the Netherlands Cancer Institute, Amsterdam, the Netherlands. a.perrakis@nki.nl.

PMID: 31270470 DOI: 10.1038/s41594-019-0254-6

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.

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