1rqi

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[[Image:1rqi.gif|left|200px]]
 
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==Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Dimethylallyl S-Thiolodiphosphate==
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The line below this paragraph, containing "STRUCTURE_1rqi", creates the "Structure Box" on the page.
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<StructureSection load='1rqi' size='340' side='right'caption='[[1rqi]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1rqi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQI FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.42&#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=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</scene>, <scene name='pdbligand=IPR:ISOPENTYL+PYROPHOSPHATE'>IPR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_1rqi| PDB=1rqi | SCENE= }}
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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=1rqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqi OCA], [https://pdbe.org/1rqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqi RCSB], [https://www.ebi.ac.uk/pdbsum/1rqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ISPA_ECOLI ISPA_ECOLI]
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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/rq/1rqi_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=1rqi ConSurf].
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<div style="clear:both"></div>
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'''Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Dimethylallyl S-Thiolodiphosphate'''
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==See Also==
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*[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Farnesyl pyrophosphate synthetase (FPPS) synthesizes farnesyl pyrophosphate through successive condensations of isopentyl pyrophosphate with dimethylallyl pyrophosphate and geranyl pyrophosphate. Nitrogen-containing bisphosphonate drugs used to treat osteoclast-mediated bone resorption and tumor-induced hypercalcemia are potent inhibitors of the enzyme. Here we present crystal structures of substrate and bisphosphonate complexes of FPPS. The structures reveal how enzyme conformational changes organize conserved active site residues to exploit metal-induced ionization and substrate positioning for catalysis. The structures further demonstrate how nitrogen-containing bisphosphonates mimic a carbocation intermediate to inhibit the enzyme. Together, these FPPS complexes provide a structural template for the design of novel inhibitors that may prove useful for the treatment of osteoporosis and other clinical indications including cancer.
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==About this Structure==
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1RQI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQI OCA].
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==Reference==
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Structural basis for bisphosphonate-mediated inhibition of isoprenoid biosynthesis., Hosfield DJ, Zhang Y, Dougan DR, Broun A, Tari LW, Swanson RV, Finn J, J Biol Chem. 2004 Mar 5;279(10):8526-9. Epub 2003 Dec 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14672944 14672944]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Geranyltranstransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Brooun A]]
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[[Category: Brooun, A.]]
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[[Category: Dougan DR]]
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[[Category: Dougan, D R.]]
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[[Category: Finn J]]
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[[Category: Finn, J.]]
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[[Category: Hosfield DJ]]
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[[Category: Hosfield, D J.]]
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[[Category: Swanson RV]]
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[[Category: Swanson, R V.]]
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[[Category: Tari LW]]
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[[Category: Tari, L W.]]
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[[Category: Zhang Y]]
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[[Category: Zhang, Y.]]
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[[Category: Isoprenyl synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:47:38 2008''
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Current revision

Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Dimethylallyl S-Thiolodiphosphate

PDB ID 1rqi

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