Rab7: crystallization of intact and C-terminal truncated constructs complexed with GDP and GppNHp.
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.
Brachvogel
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V
EMBL Heidelberg, Biological Structures and Biocomputing, Germany.
Neu
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Metcalf
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P
D018360:Crystallography, X-Ray; D019204:GTP-Binding Proteins / Q000737:chemistry*; D006153:Guanosine Diphosphate / Q000737:chemistry*; D006165:Guanylyl Imidodiphosphate / Q000737:chemistry*; D020691:rab GTP-Binding Proteins; D000090802:rab7 GTP-Binding Proteins
D000090802:rab7 GTP-Binding Proteins; D006153:Guanosine Diphosphate; D006165:Guanylyl Imidodiphosphate; D019204:GTP-Binding Proteins; D020691:rab GTP-Binding Proteins