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1fpp

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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, are based in part on the observation of electron density in the active, site which can be modeled as bound farnesyl diphosphate carried through, the enzyme purification. In addition, our model explains in structural, terms the results of mutational studies which have identified several, residues critical for substrate specificity and catalysis.
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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]. Structure known Active Site: ZN. 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 Nov 5 16:12:39 2007''
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Current revision

PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE

PDB ID 1fpp

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