1n4q

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(New page: 200px<br /><applet load="1n4q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n4q, resolution 2.40&Aring;" /> '''Protein Geranylgeran...)
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[[Image:1n4q.gif|left|200px]]<br /><applet load="1n4q" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1n4q, resolution 2.40&Aring;" />
 
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'''Protein Geranylgeranyltransferase type-I Complexed with a GGPP Analog and a KKKSKTKCVIL Peptide'''<br />
 
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==Overview==
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==Protein Geranylgeranyltransferase type-I Complexed with a GGPP Analog and a KKKSKTKCVIL Peptide==
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Protein geranylgeranyltransferase type-I (GGTase-I), one of two CaaX, prenyltransferases, is an essential enzyme in eukaryotes. GGTase-I, catalyzes C-terminal lipidation of &gt;100 proteins, including many GTP-, binding regulatory proteins. We present the first structural information, for mammalian GGTase-I, including a series of substrate and product, complexes that delineate the path of the chemical reaction. These, structures reveal that all protein prenyltransferases share a common, reaction mechanism and identify specific residues that play a dominant, role in determining prenyl group specificity. This hypothesis was, confirmed by converting farnesyltransferase (15-C prenyl substrate) into, GGTase-I (20-C prenyl substrate) with a single point mutation. GGTase-I, discriminates against farnesyl diphosphate (FPP) at the product turnover, step through the inability of a 15-C FPP to displace the 20-C, prenyl-peptide product. Understanding these key features of specificity is, expected to contribute to optimization of anti-cancer and anti-parasite, drugs.
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<StructureSection load='1n4q' size='340' side='right'caption='[[1n4q]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1n4q]] 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=1N4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N4Q FirstGlance]. <br>
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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]] 2.4&#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=MGM:2-[METHYL-(5-GERANYL-4-METHYL-PENT-3-ENYL)-AMINO]-ETHYL-DIPHOSPHATE'>MGM</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=1n4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4q OCA], [https://pdbe.org/1n4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n4q RCSB], [https://www.ebi.ac.uk/pdbsum/1n4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n4q 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/n4/1n4q_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1n4q ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein geranylgeranyltransferase type-I (GGTase-I), one of two CaaX prenyltransferases, is an essential enzyme in eukaryotes. GGTase-I catalyzes C-terminal lipidation of &gt;100 proteins, including many GTP- binding regulatory proteins. We present the first structural information for mammalian GGTase-I, including a series of substrate and product complexes that delineate the path of the chemical reaction. These structures reveal that all protein prenyltransferases share a common reaction mechanism and identify specific residues that play a dominant role in determining prenyl group specificity. This hypothesis was confirmed by converting farnesyltransferase (15-C prenyl substrate) into GGTase-I (20-C prenyl substrate) with a single point mutation. GGTase-I discriminates against farnesyl diphosphate (FPP) at the product turnover step through the inability of a 15-C FPP to displace the 20-C prenyl-peptide product. Understanding these key features of specificity is expected to contribute to optimization of anti-cancer and anti-parasite drugs.
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==About this Structure==
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Structure of mammalian protein geranylgeranyltransferase type-I.,Taylor JS, Reid TS, Terry KL, Casey PJ, Beese LS EMBO J. 2003 Nov 17;22(22):5963-74. PMID:14609943<ref>PMID:14609943</ref>
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1N4Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN, CL, TTH and MGM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N4Q OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of mammalian protein geranylgeranyltransferase type-I., Taylor JS, Reid TS, Terry KL, Casey PJ, Beese LS, EMBO J. 2003 Nov 17;22(22):5963-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14609943 14609943]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1n4q" style="background-color:#fffaf0;"></div>
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[[Category: Rattus norvegicus]]
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[[Category: Beese, L.S.]]
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[[Category: Casey, P.J.]]
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[[Category: Reid, T.S.]]
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[[Category: Taylor, J.S.]]
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[[Category: CL]]
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[[Category: MGM]]
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[[Category: TTH]]
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[[Category: ZN]]
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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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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:57:38 2007''
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==See Also==
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*[[Geranylgeranyl transferase 3D structures|Geranylgeranyl transferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Rattus norvegicus]]
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[[Category: Beese LS]]
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[[Category: Casey PJ]]
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[[Category: Reid TS]]
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[[Category: Taylor JS]]

Current revision

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

PDB ID 1n4q

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