1DCE
CRYSTAL STRUCTURE OF RAB GERANYLGERANYLTRANSFERASE FROM RAT BRAIN
Summary for 1DCE
Entry DOI | 10.2210/pdb1dce/pdb |
Descriptor | PROTEIN (RAB GERANYLGERANYLTRANSFERASE ALPHA SUBUNIT), PROTEIN (RAB GERANYLGERANYLTRANSFERASE BETA SUBUNIT), ZINC ION, ... (4 entities in total) |
Functional Keywords | rab geranylgeranyltransferase, 2.0 a resolution, n-formylmethionine, alpha subunit, beta subunit, transferase |
Biological source | Rattus norvegicus (Norway rat) More |
Total number of polymer chains | 4 |
Total formula weight | 203933.47 |
Authors | Zhang, H.,Seabra, M.C.,Deisenhofer, H. (deposition date: 1999-11-04, release date: 2000-03-24, Last modification date: 2024-10-16) |
Primary citation | Zhang, H.,Seabra, M.C.,Deisenhofer, J. Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution. Structure Fold.Des., 8:241-251, 2000 Cited by 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). PubMed: 10745007DOI: 10.1016/S0969-2126(00)00102-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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