1cq1: Difference between revisions

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[[Image:1cq1.~~gif~~|left|200px]]

[[Image:1cq1.png|left|200px]]

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~~==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 [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus]. The following page contains interesting information on the relation of 1CQ1 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb77_1.html Glucose Oxidase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQ1 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:[http://www.ncbi.nlm.nih.gov/pubmed/10508152 10508152]

[[Category: Acinetobacter calcoaceticus]]

[[Category: Glucose Oxidase]]

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[[Category: Complex with cofactor and substrate]]

[[Category: Superbarrel]]

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-[[Image:1cq1.gif|left|200px]]
+[[Image:1cq1.png|left|200px]]
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-==Overview==
+{{ABSTRACT_10508152}}
-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==
 CQ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus]. The following page contains interesting information on the relation of 1CQ1 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb77_1.html Glucose Oxidase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQ1 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:[http://www.ncbi.nlm.nih.gov/pubmed/10508152 10508152]
 [[Category: Acinetobacter calcoaceticus]]
 [[Category: Glucose Oxidase]]
@@ Line 30: / Line 26: @@
 [[Category: Complex with cofactor and substrate]]
 [[Category: Superbarrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:59:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:09:06 2008''