Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):468-71. doi: 10.1107/S1744309113007082. Epub 2013 Mar 29.

Abstract

PIST [PDZ (PSD-95, Discs-large and ZO-1) protein interacting specifically with TC10] functions as a regulator of membrane trafficking with Rab6A. Recently, the involvement of the fusion of PIST with ROS1 in cancer development has been identified. In this study, the coiled-coil domain of PIST, which is the domain responsible for interaction with Rab6A and fusion with ROS1, corresponding to amino acids 29-133, was overexpressed in Escherichia coli using engineered C-terminal His tags. The coiled-coil domain of PIST was then purified to homogeneity and crystallized at 293 K. Finally, X-ray diffraction data were collected to a resolution of 4.0 Å from a crystal belonging to the hexagonal space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 85.19, c = 240.09 Å, γ = 120.00°.

Keywords: PIST; Rab small G protein; membrane trafficking; oncogenic fusion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Golgi Matrix Proteins
  • Humans
  • Membrane Proteins / chemistry*
  • Membrane Transport Proteins

Substances

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • GOPC protein, human
  • Golgi Matrix Proteins
  • Membrane Proteins
  • Membrane Transport Proteins