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3ksl
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3ksl.jpg|left|200px]] | ||
| - | < | + | ==Structure of FPT bound to DATFP-DH-GPP== |
| - | + | <StructureSection load='3ksl' size='340' side='right'caption='[[3ksl]], [[Resolution|resolution]] 2.05Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | or the | + | <table><tr><td colspan='2'>[[3ksl]] 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=3KSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KSL 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]] 2.05Å</td></tr> | |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SZH:(2S,6E)-8-{[(R)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]OXY}-2,6-DIMETHYLOCT-6-EN-1-YL+(2S)-3,3,3-TRIFLUORO-2-HYDRAZINOPROPANOATE'>SZH</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=3ksl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ksl OCA], [https://pdbe.org/3ksl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ksl RCSB], [https://www.ebi.ac.uk/pdbsum/3ksl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ksl ProSAT]</span></td></tr> | |
| + | </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/ks/3ksl_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=3ksl ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Photoactive analogs of farnesyl diphosphate (FPP) are useful probes in studies of enzymes that employ this molecule as a substrate. Here, we describe the preparation and properties of two new FPP analogs that contain diazotrifluoropropanoyl photophores linked to geranyl diphosphate via amide or ester linkages. The amide-linked analog (3) was synthesized in 32P-labeled form from geraniol in seven steps. Experiments with Saccharomyces cerevisiae protein farnesyltransferase (ScPFTase) showed that 3 is an alternative substrate for the enzyme. Photolysis experiments with [(32)P]3 demonstrate that this compound labels the beta-subunits of both farnesyltransferase and geranylgeranyltransferase (types 1 and 2). However, the amide-linked probe 3 undergoes a rearrangement to a photochemically unreactive isomeric triazolone upon long term storage making it inconvenient to use. To address this stability issue, the ester-linked analog 4 was prepared in six steps from geraniol. Computational analysis and X-ray crystallographic studies suggest that 4 binds to protein farnesyl transferase (PFTase) in a similar fashion as FPP. Compound 4 is also an alternative substrate for PFTase, and a 32P-labeled form selectively photocrosslinks the beta-subunit of ScPFTase as well as E. coli farnesyldiphosphate synthase and a germacrene-producing sesquiterpene synthase from Nostoc sp. strain PCC7120 (a cyanobacterial source). Finally, nearly exclusive labeling of ScPFTase in crude E. coli extract was observed, suggesting that [32P]4 manifests significant selectivity and should hence be useful for identifying novel FPP-utilizing enzymes in crude protein preparations. | ||
| - | + | Synthesis, properties, and applications of diazotrifluropropanoyl-containing photoactive analogs of farnesyl diphosphate containing modified linkages for enhanced stability.,Hovlid ML, Edelstein RL, Henry O, Ochocki J, DeGraw A, Lenevich S, Talbot T, Young VG, Hruza AW, Lopez-Gallego F, Labello NP, Strickland CL, Schmidt-Dannert C, Distefano MD Chem Biol Drug Des. 2010 Jan;75(1):51-67. PMID:19954434<ref>PMID:19954434</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3ksl" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Farnesyltransferase 3D structures|Farnesyltransferase 3D structures]] | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: DeGraw | + | [[Category: DeGraw A]] |
| - | [[Category: Distefano | + | [[Category: Distefano MD]] |
| - | [[Category: Edelstein | + | [[Category: Edelstein RL]] |
| - | [[Category: Henry | + | [[Category: Henry O]] |
| - | [[Category: Hovlid | + | [[Category: Hovlid ML]] |
| - | [[Category: Hruza | + | [[Category: Hruza AW]] |
| - | [[Category: Labello | + | [[Category: Labello NP]] |
| - | [[Category: Lenevich | + | [[Category: Lenevich S]] |
| - | [[Category: Lopez-Gallego | + | [[Category: Lopez-Gallego F]] |
| - | [[Category: Ochocki | + | [[Category: Ochocki J]] |
| - | [[Category: Schmidt-Dannert | + | [[Category: Schmidt-Dannert C]] |
| - | [[Category: Strickland | + | [[Category: Strickland CL]] |
| - | [[Category: Talbot | + | [[Category: Talbot T]] |
| - | [[Category: Young | + | [[Category: Young V]] |
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Current revision
Structure of FPT bound to DATFP-DH-GPP
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Categories: Large Structures | Rattus norvegicus | DeGraw A | Distefano MD | Edelstein RL | Henry O | Hovlid ML | Hruza AW | Labello NP | Lenevich S | Lopez-Gallego F | Ochocki J | Schmidt-Dannert C | Strickland CL | Talbot T | Young V

