Rab7: crystallization of intact and C-terminal truncated constructs complexed with GDP and GppNHp

Proteins. 1997 Feb;27(2):210-2. doi: 10.1002/(sici)1097-0134(199702)27:2<210::aid-prot7>3.0.co;2-j.

Abstract

The GTP/GDP conformational switch of members of the rab family of ras-related GTP-ases control specific intracellular vesicle transport pathways. We report the crystallization of the late-endosomal rab protein rab7, in both GTP and GDP conformations. X-ray data from crystals of rab7(1-207) GppNHp (i.e., intact rab7, without C-terminal bound lipid, complexed with a non-hydrolysable GTP analog), rab7(1-197)GppNHp and rab7(1-197)GDP were collected to 1.9A (0 degree C), 1.76A (100 degrees K) and 1.75A (100 degrees K) respectively. Rab7-GDP crystals diffract to at least 1.35A.

MeSH terms

  • Crystallography, X-Ray
  • GTP-Binding Proteins / chemistry*
  • Guanosine Diphosphate / chemistry*
  • Guanylyl Imidodiphosphate / chemistry*
  • rab GTP-Binding Proteins*

Substances

  • Guanosine Diphosphate
  • rab7 protein
  • Guanylyl Imidodiphosphate
  • GTP-Binding Proteins
  • rab GTP-Binding Proteins