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 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.
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'''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<ref>PMID:16477080</ref>.
== Disease ==
== Disease ==
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== Structural highlights ==
== Structural highlights ==
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The active site with bound geranylgeranyl pyrophosphate contains a Zn+2 atom<ref>PMID:18756270</ref>.
</StructureSection>
</StructureSection>

Revision as of 10:21, 6 March 2016

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).

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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

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Michal Harel, Alexander Berchansky

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