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spinqualitylabelsall models Structure of rat geranylgeranyl transferase type 2 subunits α (grey) and β (green) complex with geranylgeranyl pyrophosphate, Zn+2 (grey) and Ca+2 (green) ions(PDB code 3dst). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights Function Geranylgeranyl transferase type 1 (GGT1) adds a 20-carbon isoprenoid group called geranylgeranyl (GG) to the C-terminal of proteins containg the CAAX motif (Cysteine, Aliphatic, Aliphatic, any amino acid). Geranylgeranyl transferase type 2 (GGT2) adds 2 GG groups to C-terminal cysteine residue of a protein. The addition of the hydrophobic prenyl group causes the proteins to become membrane-associated[1]. Disease Relevance Structural highlights The active site with bound geranylgeranyl pyrophosphate contains a Zn+2 atom[2].

3D structures of eranylgeranyl transferase

Updated on 06-March-2016

References

1. ↑ Lane KT, Beese LS. Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I. J Lipid Res. 2006 Apr;47(4):681-99. Epub 2006 Feb 13. PMID:16477080 doi:http://dx.doi.org/10.1194/jlr.R600002-JLR200
2. ↑ Guo Z, Wu YW, Das D, Delon C, Cramer J, Yu S, Thuns S, Lupilova N, Waldmann H, Brunsveld L, Goody RS, Alexandrov K, Blankenfeldt W. Structures of RabGGTase-substrate/product complexes provide insights into the evolution of protein prenylation. EMBO J. 2008 Sep 17;27(18):2444-56. Epub 2008 Aug 28. PMID:18756270 doi:10.1038/emboj.2008.164