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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1cru.gif|left|200px]]<br /><applet load="1cru" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1cru, resolution 1.50&Aring;" />
caption="1cru, resolution 1.50&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CRU OCA].  
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.W.]]
[[Category: Dijkstra, B W.]]
[[Category: Oubrie, A.]]
[[Category: Oubrie, A.]]
[[Category: Rozeboom, H.J.]]
[[Category: Rozeboom, H J.]]
[[Category: CA]]
[[Category: CA]]
[[Category: GOL]]
[[Category: GOL]]
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[[Category: superbarrel]]
[[Category: superbarrel]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:42:37 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:08 2008''