1c9u
From Proteopedia
(New page: 200px<br /><applet load="1c9u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c9u, resolution 2.20Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1c9u.gif|left|200px]]<br /><applet load="1c9u" size=" | + | [[Image:1c9u.gif|left|200px]]<br /><applet load="1c9u" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1c9u, resolution 2.20Å" /> | caption="1c9u, resolution 2.20Å" /> | ||
'''CRYSTAL STRUCTURE OF THE SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE IN COMPLEX WITH PQQ'''<br /> | '''CRYSTAL STRUCTURE OF THE SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE IN COMPLEX WITH PQQ'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Soluble glucose dehydrogenase (s-GDH; EC 1.1.99.17) is a classical | + | 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== | ==About this Structure== | ||
| - | 1C9U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus] with CA, PQQ and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Quinoprotein_glucose_dehydrogenase Quinoprotein glucose dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.5.2 1.1.5.2] Full crystallographic information is available from [http:// | + | 1C9U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=PQQ:'>PQQ</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Quinoprotein_glucose_dehydrogenase Quinoprotein glucose dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.5.2 1.1.5.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9U OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Quinoprotein glucose dehydrogenase]] | [[Category: Quinoprotein glucose dehydrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dijkstra, B | + | [[Category: Dijkstra, B W.]] |
[[Category: Oubrie, A.]] | [[Category: Oubrie, A.]] | ||
| - | [[Category: Rozeboom, H | + | [[Category: Rozeboom, H J.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: superbarrel]] | [[Category: superbarrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:03:57 2008'' |
Revision as of 10:03, 21 February 2008
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CRYSTAL STRUCTURE OF THE SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE IN COMPLEX WITH PQQ
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
1C9U is a Single protein structure of sequence from Acinetobacter calcoaceticus with , and as ligands. 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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