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{{STRUCTURE_3ksl|  PDB=3ksl  |  SCENE=  }}
==Structure of FPT bound to DATFP-DH-GPP==
===Structure of FPT bound to DATFP-DH-GPP===
<StructureSection load='3ksl' size='340' side='right' caption='[[3ksl]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
{{ABSTRACT_PUBMED_19954434}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3ksl]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KSL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Fnta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]), Fntb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_farnesyltransferase Protein farnesyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.58 2.5.1.58] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ksl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ksl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ksl RCSB], [http://www.ebi.ac.uk/pdbsum/3ksl PDBsum]</span></td></tr>
</table>
== 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/chain_selection.php?pdb_ID=2ata 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.


==Function==
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>
[[http://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.  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[3ksl]] is a 2 chain structure with sequence from [http://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].
</div>


==Reference==
==See Also==
<ref group="xtra">PMID:019954434</ref><references group="xtra"/><references/>
*[[Farnesyltransferase|Farnesyltransferase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Protein farnesyltransferase]]
[[Category: Protein farnesyltransferase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: DeGraw, A.]]
[[Category: DeGraw, A]]
[[Category: Distefano, M D.]]
[[Category: Distefano, M D]]
[[Category: Edelstein, R L.]]
[[Category: Edelstein, R L]]
[[Category: Henry, O.]]
[[Category: Henry, O]]
[[Category: Hovlid, M L.]]
[[Category: Hovlid, M L]]
[[Category: Hruza, A W.]]
[[Category: Hruza, A W]]
[[Category: Labello, N P.]]
[[Category: Labello, N P]]
[[Category: Lenevich, S.]]
[[Category: Lenevich, S]]
[[Category: Lopez-Gallego, F.]]
[[Category: Lopez-Gallego, F]]
[[Category: Ochocki, J.]]
[[Category: Ochocki, J]]
[[Category: Schmidt-Dannert, C.]]
[[Category: Schmidt-Dannert, C]]
[[Category: Strickland, C L.]]
[[Category: Strickland, C L]]
[[Category: Talbot, T.]]
[[Category: Talbot, T]]
[[Category: Young, V.]]
[[Category: Young, V]]
[[Category: Metal-binding]]
[[Category: Metal-binding]]
[[Category: Phosphoprotein]]
[[Category: Phosphoprotein]]
[[Category: Prenyltransferase]]
[[Category: Prenyltransferase]]
[[Category: Transferase]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/3ksl"