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. Epub 2019 Jul 1.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism
  • Cell Cycle Proteins / chemistry*
  • Cell Cycle Proteins / metabolism
  • Crystallography, X-Ray
  • Humans
  • Molecular Docking Simulation
  • Protein Conformation
  • Protein Domains
  • Tubulin / metabolism


  • Carrier Proteins
  • Cell Cycle Proteins
  • SVBP protein, human
  • Tubulin
  • VASH1 protein, human