1o1t
From Proteopedia
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| - | [[Image:1o1t.png|left|200px]] | ||
| - | + | ==Structure of FPT bound to the CVIM-FPP product== | |
| - | + | <StructureSection load='1o1t' size='340' side='right'caption='[[1o1t]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1o1t]] 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=1O1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O1T FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2NH:N-ACETYL-S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL]-L-CYSTEINYL-D-VALYL-L-ISOLEUCYL-L-METHIONINE'>2NH</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | == | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o1t OCA], [https://pdbe.org/1o1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o1t RCSB], [https://www.ebi.ac.uk/pdbsum/1o1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o1t ProSAT]</span></td></tr> |
| - | [[1o1t]] is a 2 chain structure with sequence from [ | + | </table> |
| + | == Function == | ||
| + | [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). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o1/1o1t_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1o1t ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Farnesyltransferase|Farnesyltransferase]] | + | *[[Farnesyltransferase 3D structures|Farnesyltransferase 3D structures]] |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | < | + | [[Category: Large Structures]] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Distefano | + | [[Category: Distefano MD]] |
| - | [[Category: Strickland | + | [[Category: Strickland CL]] |
| - | [[Category: Turek-Etienne | + | [[Category: Turek-Etienne TC]] |
| - | + | ||
| - | + | ||
Current revision
Structure of FPT bound to the CVIM-FPP product
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