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<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 ==
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The <scene name='59/597443/Cv/5'>active site with bound geranylgeranyl pyrophosphate</scene> contains a <scene name='59/597443/Cv/6'>Zn+2 atom</scene><ref>PMID:18756270</ref>. Water molecules shown as red spheres.
The <scene name='59/597443/Cv/5'>active site with bound geranylgeranyl pyrophosphate</scene> contains a <scene name='59/597443/Cv/6'>Zn+2 atom</scene><ref>PMID:18756270</ref>. Water molecules shown as red spheres.
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</StructureSection>
 
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==3D structures of eranylgeranyl transferase==
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==3D structures of geranylgeranyl transferase==
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[[Geranylgeranyl transferase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Geranylgeranyl transferase type 1
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**[[1s64]] – rGGT1 α+β subunits + inhibitor - rat<br />
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**[[1n4p]] – rGGT1 α+β subunits + GGPP<br />
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**[[1n4s]], [[1n4r]] – rGGT1 α+β subunits + GGPP + peptide-GG containing CAAX <br />
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**[[1tnb]], [[1tno]], [[1tnu]], [[1tny]], [[1tnz]], [[1n4q]] – rGGT1 α+β subunits + GGPP analog + peptide containing CAAX<br />
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**[[3dra]] – GGT1 α+β subunits + GGPP – ''Candida albicans''<br />
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*Geranylgeranyl transferase type 2
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**[[1dce]] – rGGT2 α+β subunits – rat<br />
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**[[3dss]] – rGGT2 α+β subunits <br />
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*Geranylgeranyl transferase type 2 complex
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**[[3c72]], [[3pz1]], [[3pz3]], [[4ehm]], [[4gts]], [[4gtt]], [[4gtv]] – rGGT2 α+β subunits + inhibitor<br />
 
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**[[3hxb]], [[3hxc]], [[3hxd]], [[3hxe]], [[3hxf]] – rGGT2 α (mutant) +β subunits + inhibitor<br />
 
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**[[1ltx]] – rGGT α+β subunits + tetra-alanine + Rab escort protein + farnesyl<br />
 
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**[[3dst]] – rGGT2 α+β subunits + GGPP<br />
 
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**[[3dsu]] – rGGT2 α+β subunits + farnesyl-PP<br />
 
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**[[3dsv]], [[3dsw]], [[3dsx]] – rGGT2 α+β subunits + GG<br />
 
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**[[3pz2]] – rGGT2 α+β subunits + GGPP + inhibitor<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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