2CDB

Sulfolobus solfataricus Glucose Dehydrogenase 1 in complex with NADP and glucose

Summary for 2CDB

• Entry DOI: 10.2210/pdb2cdb/pdb
• Related: 2CD9 2CDA 2CDC
• Descriptor: GLUCOSE 1-DEHYDROGENASE (DHG-1), 1,2-ETHANEDIOL, beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: reductase, oxidoreductase, mdr family
• Biological source: SULFOLOBUS SOLFATARICUS
• Total number of polymer chains: 4
• Total formula weight: 168126.80

Authors

Milburn, C.C.,Lamble, H.J.,Theodossis, A.,Hough, D.W.,Danson, M.J.,Taylor, G.L. (deposition date: 2006-01-23, release date: 2006-03-22, Last modification date: 2024-11-13)

Primary citation

Milburn, C.C.,Lamble, H.J.,Theodossis, A.,Bull, S.D.,Hough, D.W.,Danson, M.J.,Taylor, G.L.
The Structural Basis of Substrate Promiscuity in Glucose Dehydrogenase from the Hyperthermophilic Archaeon Sulfolobus Solfataricus.
J.Biol.Chem., 281:14796-, 2006

PubMed Abstract: The hyperthermophilic archaeon Sulfolobus solfataricus grows optimally above 80 degrees C and utilizes an unusual, promiscuous, non-phosphorylative Entner-Doudoroff pathway to metabolize both glucose and galactose. The first enzyme in this pathway, glucose dehydrogenase, catalyzes the oxidation of glucose to gluconate, but has been shown to have activity with a broad range of sugar substrates, including glucose, galactose, xylose, and L-arabinose, with a requirement for the glucose stereo configuration at the C2 and C3 positions. Here we report the crystal structure of the apo form of glucose dehydrogenase to a resolution of 1.8 A and a complex with its required cofactor, NADP+, to a resolution of 2.3 A. A T41A mutation was engineered to enable the trapping of substrate in the crystal. Complexes of the enzyme with D-glucose and D-xylose are presented to resolutions of 1.6 and 1.5 A, respectively, that provide evidence of selectivity for the beta-anomeric, pyranose form of the substrate, and indicate that this is the productive substrate form. The nature of the promiscuity of glucose dehydrogenase is also elucidated, and a physiological role for this enzyme in xylose metabolism is suggested. Finally, the structure suggests that the mechanism of sugar oxidation by this enzyme may be similar to that described for human sorbitol dehydrogenase.

PubMed: 16556607
DOI: 10.1074/JBC.M601334200

Experimental method

X-RAY DIFFRACTION (1.6 Å)