View source for 1v1j

==CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINTAE DEHYDRATASE FROM STREPTOMYCES COELICOLOR IN COMPLEX WITH 3-FLUORO==
<StructureSection load='1v1j' size='340' side='right' caption='[[1v1j]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1v1j]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V1J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V1J FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FA3:2-ANHYDRO-3-FLUORO-QUINIC+ACID'>FA3</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d0i|1d0i]], [[1gtz|1gtz]], [[1gu0|1gu0]], [[1gu1|1gu1]]</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>
<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=1v1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v1j OCA], [http://pdbe.org/1v1j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v1j RCSB], [http://www.ebi.ac.uk/pdbsum/1v1j 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/v1/1v1j_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>
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== Publication Abstract from PubMed ==
The fluoro analogue of the enolate intermediate in the reaction catalyzed by type II dehydroquinases has been prepared from naturally occurring (-)-quinic acid over seven steps and has been shown to be the most potent inhibitor reported to date of the type II enzyme from Mycobacterium tuberculosis.

(1R,4S,5R)-3-Fluoro-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid: the fluoro analogue of the enolate intermediate in the reaction catalyzed by type II dehydroquinases.,Frederickson M, Roszak AW, Coggins JR, Lapthorn AJ, Abell C Org Biomol Chem. 2004 Jun 7;2(11):1592-6. Epub 2004 May 6. PMID:15162210<ref>PMID:15162210</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1v1j" style="background-color:#fffaf0;"></div>

==See Also==
*[[Dehydroquinase|Dehydroquinase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: 3-dehydroquinate dehydratase]]
[[Category: Coggins, J R]]
[[Category: Lapthorn, A J]]
[[Category: Roszak, A W]]
[[Category: Aromatic amino acid biosynthesis]]
[[Category: Dehydroquinase]]
[[Category: Dhq]]
[[Category: Lyase]]
[[Category: Shikimate]]