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Rab7: Crystallization of intact and C‐terminal truncated constructs complexed with GDP and GppNHp
Author(s) -
Brachvogel Volker,
Neu Margarete,
Metcalf Peter
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199702)27:2<210::aid-prot7>3.0.co;2-j
Subject(s) - gtp' , rab , crystallization , intracellular , chemistry , gtpase , guanosine diphosphate , biophysics , biochemistry , biology , guanosine triphosphate , organic chemistry , enzyme
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 1.9Å (0°C), 1.76Å (100°K) and 1.75Å (100°K) respectively. Rab7‐GDP crystals diffract to at least 1.35Å. © 1997 Wiley‐Liss, Inc.