
Preliminary crystallographic studies of glucose dehydrogenase from the promiscuous Entner–Doudoroff pathway in the hyperthermophilic archaeon Sulfolobus solfataricus
Author(s) -
Theodossis Alex,
Milburn Christine C.,
Heyer Narinder I.,
Lamble Henry J.,
Hough David W.,
Danson Michael J.,
Taylor Garry L.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910403101x
Subject(s) - sulfolobus solfataricus , homotetramer , nad+ kinase , dehydrogenase , orthorhombic crystal system , cofactor , sulfolobus , crystallography , enzyme , biochemistry , epimer , chemistry , stereochemistry , archaea , crystal structure , protein subunit , gene
The hyperthermophilic archaeon Sulfolobus solfataricus grows optimally above 353 K and can metabolize glucose and its C4 epimer galactose via a non‐phosphorylative variant of the Entner–Doudoroff pathway involving catalytically promiscuous enzymes that can operate with both sugars. The initial oxidation step is catalysed by glucose dehydrogenase (SsGDH), which can utilize both NAD and NADP as cofactors. The enzyme operates with glucose and galactose at similar catalytic efficiency, while its substrate profile also includes a range of other five‐ and six‐carbon sugars. Crystals of the 164 kDa SsGDH homotetramer have been grown under a variety of conditions. The best crystals to date diffract to 1.8 Å on a synchrotron source, have orthorhombic symmetry and belong to space group P 2 1 2 1 2. Attempts are being made to solve the structure by MAD and MR.