View source for 3jyo


==Quinate dehydrogenase from Corynebacterium glutamicum in complex with NAD==
<StructureSection load='3jyo' size='340' side='right'caption='[[3jyo]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3jyo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum_ATCC_13032 Corynebacterium glutamicum ATCC 13032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JYO 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]] 1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=3jyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jyo OCA], [https://pdbe.org/3jyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jyo RCSB], [https://www.ebi.ac.uk/pdbsum/3jyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jyo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AROE_CORGL AROE_CORGL] Catalyzes the NAD(+)-dependent oxidation of both quinate and shikimate to 3-dehydroquinate and 3-dehydroshikimate, respectively. Seems to play a key role in the quinate degradation pathway.<ref>PMID:18566515</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Abstract Quinate dehydrogenase (QDH) catalyzes the reversible oxidation of quinate to 3-dehydroquinate by NADH and is involved in the catabolic quinate metabolism required for the degradation of lignin. The enzyme is a member of the family of shikimate/quinate dehydrogenases (SDH/QDH) occurring in bacteria and plants. We characterized the dual-substrate quinate/shikimate dehydrogenase QSDH from Corynebacterium glutamicum (CglQSDH) kinetically and revealed a clear substrate preference of CglQSDH for quinate compared to shikimate both at the pH-optimum and in a physiological pH-range, which is a remarkable contrast to closely related SDH/QDH enzymes. With respect to the cosubstrate CglQSDH is strictly NAD(H) dependent. These substrate and cosubstrate profiles correlate nicely to the details of three atomic resolution crystal structures of CglQSDH in different functional states we report here: with bound NAD+ (binary complex) and as ternary complexes with NADH plus either shikimate or quinate. The CglQSDH-NADH-quinate structure is the first complex structure of any member of the SDH/QDH family with quinate. Based on this novel structural information and systematic sequence and structure comparisons with closely related enzymes we can explain the strict NAD(H) dependency of CglQSDH as well as its discrimination between shikimate and quinate.

Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity and discrimination.,Hoppner A, Schomburg D, Niefind K Biol Chem. 2013 Aug 8. pii:, /j/bchm.just-accepted/hsz-2013-0170/hsz-2013-0170.xml. doi:, 10.1515/hsz-2013-0170. PMID:23929881<ref>PMID:23929881</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3jyo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Shikimate dehydrogenase 3D structures|Shikimate dehydrogenase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Corynebacterium glutamicum ATCC 13032]]
[[Category: Large Structures]]
[[Category: Hoeppner A]]
[[Category: Niefind K]]
[[Category: Schomburg D]]