Fig. 1: Structure of the VASH1-SVBP complex.
From: Structural insights into tubulin detyrosination by vasohibins-SVBP complex
a Overall structure of the VASH144–315-SVBP1–66 heterodimer. VASH1 and SVBP are colored in green and cyan, respectively. Their secondary structures, N- and C-termini are labeled. Two vertical views are shown. b, c In vitro detyrosination activity assay of wildtype and mutated forms of VASH1-SVBP complex. The enzymes were incubated with purified tubulin dimer (b) or α-tubulin tail GST fusion proteins (c) for 1 h and 2 h, respectively. d Electrostatic surface representation of the VASH144–315-SVBP1–66 heterodimer. The residues whose mutation caused markedly decrease, slight decrease and no obvious decrease in activity in (b) and (c) are colored in black, yellow and red, respectively. e, f Two interfaces of VASH1-SVBP interaction are shown in cartoon. The residues involved in the interaction are shown as sticks and colored as in (a). Hydrogen bonds are shown as red dashed lines and water molecules are shown as red spheres. g, h In vitro detyrosination activity assay of wildtype and mutated forms of VASH1-SVBP complex. The enzymes were incubated with purified tubulin dimer (g) or GST-TUBA1A-C fusion proteins (h) for 1 h and 2 h, respectively.
