6NVQ

Crystal structure of the VASH1-SVBP complex

Summary for 6NVQ

• Entry DOI: 10.2210/pdb6nvq/pdb
• Descriptor: Tubulinyl-Tyr carboxypeptidase 1, Small vasohibin-binding protein, GLYCEROL, ... (4 entities in total)
• Functional Keywords: tyrosine carboxypeptidase, hydrolase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 44444.62

Authors

Adamopoulos, A.,Perrakis, A.,Heidebrecht, T. (deposition date: 2019-02-05, release date: 2019-05-22, Last modification date: 2024-05-15)

Primary 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.
Crystal structure of the tubulin tyrosine carboxypeptidase complex VASH1-SVBP.
Nat.Struct.Mol.Biol., 26:567-570, 2019

PubMed 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.

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)