View source for 3zok


==Structure of 3-Dehydroquinate Synthase from Actinidia chinensis in complex with NAD==
<StructureSection load='3zok' size='340' side='right'caption='[[3zok]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zok]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinidia_chinensis Actinidia chinensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZOK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=3zok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zok OCA], [https://pdbe.org/3zok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zok RCSB], [https://www.ebi.ac.uk/pdbsum/3zok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zok ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DHQS_ACTCC DHQS_ACTCC] Catalyzes the second step in the shikimate pathway.<ref>PMID:23916589</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
One of the novel aspects of kiwifruit is the presence of high level of quinic acid which contributes to the flavour of the fruit. Quinic acid metabolism intersects with the shikimate pathway, which is responsible for the de novo biosynthesis of primary and secondary aromatic metabolites. The gene encoding the enzyme which catalyses the second step of the shikimate pathway, dehydroquinate synthase (DHQS), from the New Zealand kiwifruit Actinidia chinensis was identified, cloned and expressed. A. chinensis DHQS was activated by divalent metal ions, and was found to require NAD+ for catalysis. The protein was crystallised and the structure was solved, revealing a homodimeric protein. Each monomer has a NAD+ binding site nestled between the distinct N- and C-terminal domains. In contrast to other microbial DHQSs, which show an open conformation in the absence of active site ligands, A. chinensis DHQS adopts a closed conformation. This is the first report of the structure of a DHQS from a plant source.

Biochemical and structural characterisation of dehydroquinate synthase from the New Zealand kiwifruit Actinidia chinensis.,Mittelstadt G, Negron L, Schofield LR, Marsh K, Parker EJ Arch Biochem Biophys. 2013 Aug 2. pii: S0003-9861(13)00229-4. doi:, 10.1016/j.abb.2013.07.022. PMID:23916589<ref>PMID:23916589</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zok" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actinidia chinensis]]
[[Category: Large Structures]]
[[Category: Marsh K]]
[[Category: Mittelstaedt G]]
[[Category: Negron L]]
[[Category: Parker EJ]]
[[Category: Schofield LR]]