1cru
From Proteopedia
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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 CA, PQQ, PQQ, HDN and GOL 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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