1cq1

<table><tr><td colspan='2'>[[1cq1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acica Acica]. The May 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Glucose Oxidase'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_5 10.2210/rcsb_pdb/mom_2006_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CQ1 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qbi|1qbi]], [[1c9u|1c9u]], [[1cru|1cru]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Quinoprotein_glucose_dehydrogenase_(PQQ,_quinone) Quinoprotein glucose dehydrogenase (PQQ, quinone)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.5.2 1.1.5.2] </span></td></tr>

[[https://www.uniprot.org/uniprot/DHGB_ACICA DHGB_ACICA]] Oxidizes glucose to gluconolactone.

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== Publication Abstract from PubMed ==

Soluble glucose dehydrogenase (s-GDH; EC 1.1.99.17) is a classical quinoprotein which requires the cofactor pyrroloquinoline quinone (PQQ) to oxidize glucose to gluconolactone. The reaction mechanism of PQQ-dependent enzymes has remained controversial due to the absence of comprehensive structural data. We have determined the X-ray structure of s-GDH with the cofactor at 2.2 A resolution, and of a complex with reduced PQQ and glucose at 1.9 A resolution. These structures reveal the active site of s-GDH, and show for the first time how a functionally bound substrate interacts with the cofactor in a PQQ-dependent enzyme. Twenty years after the discovery of PQQ, our results finally provide conclusive evidence for a reaction mechanism comprising general base-catalyzed hydride transfer, rather than the generally accepted covalent addition-elimination mechanism. Thus, PQQ-dependent enzymes use a mechanism similar to that of nicotinamide- and flavin-dependent oxidoreductases.

Structure and mechanism of soluble quinoprotein glucose dehydrogenase.,Oubrie A, Rozeboom HJ, Kalk KH, Olsthoorn AJ, Duine JA, Dijkstra BW EMBO J. 1999 Oct 1;18(19):5187-94. PMID:10508152<ref>PMID:10508152</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 1cq1" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Acica]]

[[Category: Dijkstra, B W]]

[[Category: Oubrie, A]]

[[Category: Rozeboom, H J]]

[[Category: Superbarrel]]