6hs8: Difference between revisions

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 <StructureSection load='6hs8' size='340' side='right'caption='[[6hs8]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6hs8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HS8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HS8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6hs8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Butyrivibrio_crossotus_DSM_2876 Butyrivibrio crossotus DSM 2876]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HS8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></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=6hs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hs8 OCA], [http://pdbe.org/6hs8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hs8 RCSB], [http://www.ebi.ac.uk/pdbsum/6hs8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hs8 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6hs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hs8 OCA], [https://pdbe.org/6hs8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hs8 RCSB], [https://www.ebi.ac.uk/pdbsum/6hs8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hs8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/D4S0D1_9FIRM D4S0D1_9FIRM]] Catalyzes a trans-dehydration via an enolate intermediate.[HAMAP-Rule:MF_00169]
+[https://www.uniprot.org/uniprot/D4S0D1_9FIRM D4S0D1_9FIRM] Catalyzes a trans-dehydration via an enolate intermediate.[HAMAP-Rule:MF_00169]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
--Dehydroquinate dehydratase (DHQase) catalyzes the conversion of 3-dehydroquinic acid to 3-dehydroshikimic acid of the shikimate pathway. In this study, 3180 prokaryotic genomes were examined and 459 DHQase sequences were retrieved. Based on sequence analysis and their original hosts, 38 DHQase genes were selected for chemical synthesis. The selected DHQases were translated into new DNA sequences according to the genetic codon usage bias by both Escherichia coli and Corynebacterium glutamicum. The new DNA sequences were customized for synthetic biological applications by adding Biobrick adapters at both ends and by removal of any related restriction endonuclease sites. The customized DHQase genes were successfully expressed in E. coli, and functional DHQases were obtained. Kinetic parameters of Km, kcat, and Vmax of DHQases were determined with a newly established high-throughput method for DHQase activity assay. Results showed that DHQases possessed broad strength of substrate affinities and catalytic capacities. In addition to the DHQase kinetic diversities, this study generated a DHQase library with known catalytic constants that could be applied to design artificial modules of shikimate pathway for metabolic engineering and synthetic biology.
-Unraveling the kinetic diversity of microbial 3-dehydroquinate dehydratases of shikimate pathway.,Liu C, Liu YM, Sun QL, Jiang CY, Liu SJ AMB Express. 2015 Feb 1;5:7. doi: 10.1186/s13568-014-0087-y. eCollection 2015. PMID:25852984<ref>PMID:25852984</ref>
+==See Also==
+*[[Dehydroquinase 3D structures|Dehydroquinase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6hs8" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: 3-dehydroquinate dehydratase]]
+[[Category: Butyrivibrio crossotus DSM 2876]]
 [[Category: Large Structures]]
-[[Category: Lapthorn, A J]]
+[[Category: Lapthorn AJ]]
-[[Category: Roszak, A W]]
+[[Category: Roszak AW]]
-[[Category: Biosynthetic protein]]
-[[Category: Dehydratase]]
-[[Category: Shikimate pathway]]