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 |
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Hauptverfasser: | , , , , , , , , , |
Format: | Artikel |
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. |
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ISSN: | 1545-9993 1545-9985 |
DOI: | 10.1038/s41594-019-0254-6 |