4ph6

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'''Unreleased structure'''
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==Structure of 3-Dehydroquinate Dehydratase from Enterococcus faecalis==
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<StructureSection load='4ph6' size='340' side='right' caption='[[4ph6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ph6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PH6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PH6 FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-dehydroquinate_dehydratase 3-dehydroquinate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.10 4.2.1.10] </span></td></tr>
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<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=4ph6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ph6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ph6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ph6 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Due to the emergence of resistance toward current antibiotics, there is a pressing need to develop the next generation of antibiotics as therapeutics against infectious and opportunistic diseases of microbial origins. The shikimate pathway is exclusive to microbes, plants and fungi, and hence is an attractive and logical target for development of antimicrobial therapeutics. The Gram-positive commensal microbe, Enterococcus faecalis, is a major human pathogen associated with nosocomial infections and resistance to vancomycin, the "drug of last resort". Here, we report the identification of several polyketide-based inhibitors against the E. faecalis shikimate pathway enzyme, 3-dehydroquinate dehydratase (DHQase). In particular, marein, a flavonoid polyketide, both inhibited DHQase and retarded the growth of Enterococcus faecalis. The purification, crystallization and structural resolution of recombinant DHQase from E. faecalis (at 2.2 A resolution) are also reported. This study provides a route in the development of polyketide-based antimicrobial inhibitors targeting the shikimate pathway of the human pathogen E. faecalis.
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The entry 4ph6 is ON HOLD until Paper Publication
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Identification of polyketide inhibitors targeting 3-dehydroquinate dehydratase in the shikimate pathway of Enterococcus faecalis.,Cheung VW, Xue B, Hernandez-Valladares M, Go MK, Tung A, Aguda AH, Robinson RC, Yew WS PLoS One. 2014 Jul 29;9(7):e103598. doi: 10.1371/journal.pone.0103598., eCollection 2014. PMID:25072253<ref>PMID:25072253</ref>
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Authors: Xue, B., Cheung, V.W., Yew, W.S., Robinson, R.C.
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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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Description: Structure of 3-Dehydroquinate Dehydratase from Enterococcus faecalis
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: 3-dehydroquinate dehydratase]]
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[[Category: Cheung, V W]]
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[[Category: Robinson, R C]]
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[[Category: Xue, B]]
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[[Category: Yew, W S]]
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[[Category: Lyase]]

Revision as of 08:57, 5 January 2015

Structure of 3-Dehydroquinate Dehydratase from Enterococcus faecalis

4ph6, resolution 2.20Å

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