Geranylgeranyl transferase

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== Function ==
== Function ==
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'''Geranylgeranyl transferase''' type 1 (GGT1) adds a 20-carbon isoprenoid group called geranylgeranyl (GG) to the C-terminal of proteins containing 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<ref>PMID:16477080</ref>.
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'''Geranylgeranyl transferase''' '''type 1''' (GGT1) adds a 20-carbon isoprenoid group called geranylgeranyl (GG) to the C-terminal of proteins containing 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<ref>PMID:16477080</ref>.
== Relevance ==
== Relevance ==

Current revision

Structure of rat geranylgeranyl transferase type 2 subunits α (magenta) and β (cyan) complex with geranylgeranyl pyrophosphate, Zn+2 (grey) and Ca+2 (green) ions (PDB code 3dst).

Drag the structure with the mouse to rotate

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. ↑ Lawson MA, Coulton L, Ebetino FH, Vanderkerken K, Croucher PI. Geranylgeranyl transferase type II inhibition prevents myeloma bone disease. Biochem Biophys Res Commun. 2008 Dec 12;377(2):453-7. doi:, 10.1016/j.bbrc.2008.09.157. Epub 2008 Oct 16. PMID:18929536 doi:http://dx.doi.org/10.1016/j.bbrc.2008.09.157
  3. ↑ 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

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Michal Harel, Alexander Berchansky

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