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1n4s

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{{STRUCTURE_1n4s| PDB=1n4s | SCENE= }}
 
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===Protein Geranylgeranyltransferase type-I Complexed with GGPP and a Geranylgeranylated KKKSKTKCVIL Peptide Product===
 
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{{ABSTRACT_PUBMED_14609943}}
 
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==Function==
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==Protein Geranylgeranyltransferase type-I Complexed with GGPP and a Geranylgeranylated KKKSKTKCVIL Peptide Product==
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[[http://www.uniprot.org/uniprot/FNTA_RAT FNTA_RAT]] Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK (By similarity). [[http://www.uniprot.org/uniprot/PGTB1_RAT PGTB1_RAT]] Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. Acts on the Rac1, Rac2, Rap1A and Rap1B proteins. The beta subunit is responsible for peptide-binding.
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<StructureSection load='1n4s' size='340' side='right'caption='[[1n4s]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1n4s]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N4S FirstGlance]. <br>
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[[1n4s]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4S OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GER:GERAN-8-YL+GERAN'>GER</scene>, <scene name='pdbligand=GRG:GERANYLGERANYL+DIPHOSPHATE'>GRG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4s OCA], [https://pdbe.org/1n4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n4s RCSB], [https://www.ebi.ac.uk/pdbsum/1n4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n4s ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FNTA_RAT FNTA_RAT] Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n4/1n4s_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n4s ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Farnesyltransferase|Farnesyltransferase]]
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*[[Farnesyltransferase 3D structures|Farnesyltransferase 3D structures]]
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*[[Geranylgeranyl transferase 3D structures|Geranylgeranyl transferase 3D structures]]
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==Reference==
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__TOC__
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<ref group="xtra">PMID:014609943</ref><references group="xtra"/><references/>
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Beese, L S.]]
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[[Category: Beese LS]]
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[[Category: Casey, P J.]]
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[[Category: Casey PJ]]
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[[Category: Reid, T S.]]
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[[Category: Reid TS]]
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[[Category: Taylor, J S.]]
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[[Category: Taylor JS]]
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[[Category: Caax]]
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[[Category: Geranylgeranyl]]
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[[Category: Ggtase]]
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[[Category: Lipid modification]]
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[[Category: Protein geranylgeranyltransferase type-i]]
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[[Category: Protein prenylation]]
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[[Category: Rap2b]]
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[[Category: Transferase]]
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Current revision

Protein Geranylgeranyltransferase type-I Complexed with GGPP and a Geranylgeranylated KKKSKTKCVIL Peptide Product

PDB ID 1n4s

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