TY - JOUR
T1 - Crystal structure of the tubulin tyrosine carboxypeptidase complex VASH1–SVBP
AU - Adamopoulos, Athanassios
AU - Landskron, Lisa
AU - Heidebrecht, Tatjana
AU - Tsakou, Foteini
AU - Bleijerveld, Onno B.
AU - Altelaar, Maarten
AU - Nieuwenhuis, Joppe
AU - Celie, Patrick H.N.
AU - Brummelkamp, Thijn R.
AU - Perrakis, Anastassis
PY - 2019/7/1
Y1 - 2019/7/1
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/85068401857
U2 - 10.1038/s41594-019-0254-6
DO - 10.1038/s41594-019-0254-6
M3 - Article
C2 - 31270470
AN - SCOPUS:85068401857
SN - 1545-9993
VL - 26
SP - 567
EP - 570
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
IS - 7
ER -