1fpp

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(New page: 200px<br /> <applet load="1fpp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fpp, resolution 2.75&Aring;" /> '''PROTEIN FARNESYLTRA...)
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[[Image:1fpp.gif|left|200px]]<br />
 
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<applet load="1fpp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fpp, resolution 2.75&Aring;" />
 
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'''PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE'''<br />
 
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==Overview==
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==PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE==
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The rat protein farnesyltransferase crystal structure has been solved by, multiple isomorphous replacement methods at a resolution of 2.75 A. The, three-dimensional structure, together with recent data on the effects of, several mutations, led us to propose a model for substrate binding which, differs from the model presented by Park et al. based on their independent, structure determination [Park, H. -W., Boduluri, S. R., Moomaw, J. F., Casey, P. J., and Beese, L. S. (1997) Science 275, 1800-1804]. Both, farnesyl diphosphate and peptide substrates can be accommodated in the, hydrophobic active-site barrel, with the sole charged residue inside the, barrel, Arg202 of the beta-subunit, forming a salt bridge with the, negatively charged carboxy terminus of peptide substrates. Our proposals, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9609683 (full description)]]
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<StructureSection load='1fpp' size='340' side='right'caption='[[1fpp]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fpp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FPP 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]] 2.75&#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=FPP:FARNESYL+DIPHOSPHATE'>FPP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1fpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpp OCA], [https://pdbe.org/1fpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fpp RCSB], [https://www.ebi.ac.uk/pdbsum/1fpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fpp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FNTB_RAT FNTB_RAT] Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
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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/fp/1fpp_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=1fpp ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FPP 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, PO4 and FPP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FPP OCA]].
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*[[Farnesyltransferase 3D structures|Farnesyltransferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Protein farnesyltransferase: structure and implications for substrate binding., Dunten P, Kammlott U, Crowther R, Weber D, Palermo R, Birktoft J, Biochemistry. 1998 Jun 2;37(22):7907-12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9609683 9609683]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Birktoft, J.]]
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[[Category: Birktoft J]]
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[[Category: Crowther, R.]]
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[[Category: Crowther R]]
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[[Category: Dunten, P.]]
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[[Category: Dunten P]]
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[[Category: Kammlott, U.]]
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[[Category: Kammlott U]]
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[[Category: Palermo, R.]]
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[[Category: Palermo R]]
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[[Category: Weber, D.]]
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[[Category: Weber D]]
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[[Category: FPP]]
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[[Category: PO4]]
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[[Category: ZN]]
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[[Category: heterodimer]]
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[[Category: membrane localization]]
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[[Category: prenyltransferase]]
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[[Category: zinc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:49:56 2007''
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Current revision

PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE

PDB ID 1fpp

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