Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution.
Zhang, H., Seabra, M.C., Deisenhofer, J.(2000) Structure 8: 241-251
- PubMed: 10745007 
- DOI: https://doi.org/10.1016/s0969-2126(00)00102-7
- Primary Citation of Related Structures:  
1DCE - PubMed Abstract: 
Rab geranylgeranyltransferase (RabGGT) catalyzes the addition of two geranylgeranyl groups to the C-terminal cysteine residues of Rab proteins, which is crucial for membrane association and function of these proteins in intracellular vesicular trafficking. Unlike protein farnesyltransferase (FT) and type I geranylgeranyltransferase, which both prenylate monomeric small G proteins or short peptides, RabGGT can prenylate Rab only when Rab is in a complex with Rab escort protein (REP).
Organizational Affiliation: 
Department of Biochemistry, Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center, Dallas, 75235-9050, USA.