Crystal structure of the tubulin tyrosine carboxypeptidase complex VASH1–SVBP

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 protei...

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Veröffentlicht in:Nature structural & molecular biology 2019-07, Vol.26 (7), p.567-570
Hauptverfasser: Adamopoulos, Athanassios, Landskron, Lisa, Heidebrecht, Tatjana, Tsakou, Foteini, Bleijerveld, Onno B., Altelaar, Maarten, Nieuwenhuis, Joppe, Celie, Patrick H. N., Brummelkamp, Thijn R., Perrakis, Anastassis
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Sprache:eng
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Zusammenfassung: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. Crystal structure of the tubulin carboxypeptidase complex between vasohibin and SVBP, combined with mutagenesis, reveals the residues responsible for substrate recognition and cleavage.
ISSN:1545-9993
1545-9985
DOI:10.1038/s41594-019-0254-6