1cru
From Proteopedia
(New page: 200px<br /><applet load="1cru" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cru, resolution 1.50Å" /> '''SOLUBLE QUINOPROTEIN...) |
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| - | [[Image:1cru.gif|left|200px]]<br /><applet load="1cru" size=" | + | [[Image:1cru.gif|left|200px]]<br /><applet load="1cru" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cru, resolution 1.50Å" /> | caption="1cru, resolution 1.50Å" /> | ||
'''SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE'''<br /> | '''SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Soluble glucose dehydrogenase (s-GDH) from the bacterium Acinetobacter | + | Soluble glucose dehydrogenase (s-GDH) from the bacterium Acinetobacter calcoaceticus is a classical quinoprotein. It requires the cofactor pyrroloquinoline quinone (PQQ) to catalyze the oxidation of glucose to gluconolactone. The precise catalytic role of PQQ in s-GDH and several other PQQ-dependent enzymes has remained controversial because of the absence of comprehensive structural data. We have determined the crystal structure of a ternary complex of s-GDH with PQQ and methylhydrazine, a competitive inhibitor of the enzyme. This complex, refined at 1.5-A resolution to an R factor of 16.7%, affords a detailed view of a cofactor-binding site of s-GDH. Moreover, it presents the first direct observation of covalent PQQ adduct in the active-site of a PQQ-dependent enzyme, thereby confirming previous evidence that the C5 carbonyl group of the cofactor is the most reactive moiety of PQQ. |
==About this Structure== | ==About this Structure== | ||
| - | 1CRU 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, PQQ, HDN 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:// | + | 1CRU 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>, <scene name='pdbligand=PQQ:'>PQQ</scene>, <scene name='pdbligand=HDN:'>HDN</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=1CRU 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 12:09:08 2008'' |
Revision as of 10:09, 21 February 2008
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SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE
Overview
Soluble glucose dehydrogenase (s-GDH) from the bacterium Acinetobacter calcoaceticus is a classical quinoprotein. It requires the cofactor pyrroloquinoline quinone (PQQ) to catalyze the oxidation of glucose to gluconolactone. The precise catalytic role of PQQ in s-GDH and several other PQQ-dependent enzymes has remained controversial because of the absence of comprehensive structural data. We have determined the crystal structure of a ternary complex of s-GDH with PQQ and methylhydrazine, a competitive inhibitor of the enzyme. This complex, refined at 1.5-A resolution to an R factor of 16.7%, affords a detailed view of a cofactor-binding site of s-GDH. Moreover, it presents the first direct observation of covalent PQQ adduct in the active-site of a PQQ-dependent enzyme, thereby confirming previous evidence that the C5 carbonyl group of the cofactor is the most reactive moiety of PQQ.
About this Structure
1CRU 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
Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: a covalent cofactor-inhibitor complex., Oubrie A, Rozeboom HJ, Dijkstra BW, Proc Natl Acad Sci U S A. 1999 Oct 12;96(21):11787-91. PMID:10518528
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