1CRU

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

Summary for 1CRU

• Entry DOI: 10.2210/pdb1cru/pdb
• Related: 1C9U 1CQ1 1QBI
• Descriptor: PROTEIN (SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE), CALCIUM ION, PYRROLOQUINOLINE QUINONE, ... (6 entities in total)
• Functional Keywords: beta-propeller, superbarrel, complex with the cofactor pqq and the inhibitor methylhydrazine, oxidoreductase
• Biological source: Acinetobacter calcoaceticus
• Total number of polymer chains: 2
• Total formula weight: 101667.50

Authors

Oubrie, A.,Rozeboom, H.J.,Dijkstra, B.W. (deposition date: 1999-08-16, release date: 2000-03-01, Last modification date: 2024-10-09)

Primary citation

Oubrie, A.,Rozeboom, H.J.,Dijkstra, B.W.
Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: a covalent cofactor-inhibitor complex.
Proc.Natl.Acad.Sci.USA, 96:11787-11791, 1999

PubMed Abstract: 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.

PubMed: 10518528
DOI: 10.1073/pnas.96.21.11787

Experimental method

X-RAY DIFFRACTION (1.5 Å)