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1cru

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{{STRUCTURE_1cru| PDB=1cru | SCENE= }}
{{STRUCTURE_1cru| PDB=1cru | SCENE= }}
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'''SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE'''
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===SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10518528 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10518528}}
==About this Structure==
==About this Structure==
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Superbarrel]]
[[Category: Superbarrel]]
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Revision as of 18:14, 30 June 2008

Template:STRUCTURE 1cru

SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE

Template:ABSTRACT PUBMED 10518528

About this Structure

1CRU is a Single protein structure of sequence from Acinetobacter calcoaceticus. 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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