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Crystal structure of the tubulin tyrosine carboxypeptidase complex VASH1-SVBP.

Athanassios AdamopoulosLisa LandskronTatjana HeidebrechtFoteini TsakouOnno B BleijerveldMaarten AltelaarJoppe NieuwenhuisPatrick H N CelieThijn R BrummelkampAnastassis Perrakis
Published in: Nature structural & molecular biology (2019)
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.
Keyphrases
  • molecular docking
  • binding protein
  • molecular dynamics simulations
  • dna binding
  • crispr cas
  • solid state