2e9c

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[[Image:2e9c.jpg|left|200px]]
 
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{{Structure
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==E. coli undecaprenyl pyrophosphate synthase in complex with BPH-675==
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|PDB= 2e9c |SIZE=350|CAPTION= <scene name='initialview01'>2e9c</scene>, resolution 2.05&Aring;
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<StructureSection load='2e9c' size='340' side='right'caption='[[2e9c]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=B75:1-HYDROXY-2-[3&#39;-(NAPHTHALENE-2-SULFONYLAMINO)-BIPHENYL-3-YL]ETHYLIDENE-1,1-BISPHOSPHONIC+ACID'>B75</scene>
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<table><tr><td colspan='2'>[[2e9c]] 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=2E9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E9C FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Di-trans,poly-cis-decaprenylcistransferase Di-trans,poly-cis-decaprenylcistransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.31 2.5.1.31] </span>
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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]] 2.05&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B75:1-HYDROXY-2-[3-(NAPHTHALENE-2-SULFONYLAMINO)-BIPHENYL-3-YL]ETHYLIDENE-1,1-BISPHOSPHONIC+ACID'>B75</scene></td></tr>
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|DOMAIN=
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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=2e9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e9c OCA], [https://pdbe.org/2e9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e9c RCSB], [https://www.ebi.ac.uk/pdbsum/2e9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e9c ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1x06|1X06]], [[1x07|1X07]], [[1x08|1X08]], [[1x09|1X09]], [[2e98|2E98]], [[2e99|2E99]], [[2e9a|2E9A]], [[2e9d|2E9D]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e9c OCA], [http://www.ebi.ac.uk/pdbsum/2e9c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e9c RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/UPPS_ECOLI UPPS_ECOLI] Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate (FPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.<ref>PMID:12756244</ref>
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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/e9/2e9c_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=2e9c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bisphosphonate drugs (e.g., Fosamax and Zometa) are thought to act primarily by inhibiting farnesyl diphosphate synthase (FPPS), resulting in decreased prenylation of small GTPases. Here, we show that some bisphosphonates can also inhibit geranylgeranyl diphosphate synthase (GGPPS), as well as undecaprenyl diphosphate synthase (UPPS), a cis-prenyltransferase of interest as a target for antibacterial therapy. Our results on GGPPS (10 structures) show that there are three bisphosphonate-binding sites, consisting of FPP or isopentenyl diphosphate substrate-binding sites together with a GGPP product- or inhibitor-binding site. In UPPS, there are a total of four binding sites (in five structures). These results are of general interest because they provide the first structures of GGPPS- and UPPS-inhibitor complexes, potentially important drug targets, in addition to revealing a remarkably broad spectrum of binding modes not seen in FPPS inhibition.
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'''E. coli undecaprenyl pyrophosphate synthase in complex with BPH-675'''
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Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases.,Guo RT, Cao R, Liang PH, Ko TP, Chang TH, Hudock MP, Jeng WY, Chen CK, Zhang Y, Song Y, Kuo CJ, Yin F, Oldfield E, Wang AH Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):10022-7. Epub 2007 May 29. PMID:17535895<ref>PMID:17535895</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2e9c" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Bisphosphonate drugs (e.g., Fosamax and Zometa) are thought to act primarily by inhibiting farnesyl diphosphate synthase (FPPS), resulting in decreased prenylation of small GTPases. Here, we show that some bisphosphonates can also inhibit geranylgeranyl diphosphate synthase (GGPPS), as well as undecaprenyl diphosphate synthase (UPPS), a cis-prenyltransferase of interest as a target for antibacterial therapy. Our results on GGPPS (10 structures) show that there are three bisphosphonate-binding sites, consisting of FPP or isopentenyl diphosphate substrate-binding sites together with a GGPP product- or inhibitor-binding site. In UPPS, there are a total of four binding sites (in five structures). These results are of general interest because they provide the first structures of GGPPS- and UPPS-inhibitor complexes, potentially important drug targets, in addition to revealing a remarkably broad spectrum of binding modes not seen in FPPS inhibition.
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*[[Undecaprenyl pyrophosphate synthase|Undecaprenyl pyrophosphate synthase]]
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== References ==
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==About this Structure==
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<references/>
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2E9C 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=2E9C OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases., Guo RT, Cao R, Liang PH, Ko TP, Chang TH, Hudock MP, Jeng WY, Chen CK, Zhang Y, Song Y, Kuo CJ, Yin F, Oldfield E, Wang AH, Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):10022-7. Epub 2007 May 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17535895 17535895]
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[[Category: Di-trans,poly-cis-decaprenylcistransferase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cao, R.]]
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[[Category: Cao R]]
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[[Category: Guo, R T.]]
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[[Category: Guo RT]]
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[[Category: Ko, T P.]]
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[[Category: Ko TP]]
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[[Category: Liang, P H.]]
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[[Category: Liang PH]]
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[[Category: Oldfield, E.]]
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[[Category: Oldfield E]]
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[[Category: Wang, A H.J.]]
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[[Category: Wang AHJ]]
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[[Category: antibiotic]]
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[[Category: bisphosphonate]]
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[[Category: cell wall]]
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[[Category: farnesyl pyrophosphate]]
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[[Category: prenyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:45:39 2008''
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Current revision

E. coli undecaprenyl pyrophosphate synthase in complex with BPH-675

PDB ID 2e9c

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