1cq1
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(New page: 200px<br /> <applet load="1cq1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cq1, resolution 1.9Å" /> '''SOLUBLE QUINOPROTEIN...)
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Revision as of 06:51, 18 November 2007
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SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQH2 AND GLUCOSE
Overview
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.
About this Structure
1CQ1 is a Single protein structure of sequence from Acinetobacter calcoaceticus with GLC, CA and PQQ as ligands. The following page contains interesting information on the relation of 1CQ1 with [Glucose Oxidase]. Active as Quinoprotein glucose dehydrogenase, with EC number 1.1.5.2 Full crystallographic information is available from OCA.
Reference
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
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