1GCO

CRYSTAL STRUCTURE OF GLUCOSE DEHYDROGENASE COMPLEXED WITH NAD+

Summary for 1GCO

• Entry DOI: 10.2210/pdb1gco/pdb
• Descriptor: GLUCOSE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: short-chain dehydrogenase/reductase, oxidoreductase
• Biological source: Bacillus megaterium
• Total number of polymer chains: 4
• Total formula weight: 115105.55

Authors

Yamamoto, K.,Kurisu, G.,Kusunoki, M.,Tabata, S.,Urabe, I.,Osaki, S. (deposition date: 2000-08-07, release date: 2001-02-28, Last modification date: 2023-12-27)

Primary citation

Yamamoto, K.,Kurisu, G.,Kusunoki, M.,Tabata, S.,Urabe, I.,Osaki, S.
Crystal structure of glucose dehydrogenase from Bacillus megaterium IWG3 at 1.7 A resolution.
J.Biochem., 129:303-312, 2001

PubMed Abstract: The crystal structure of glucose dehydrogenase (GlcDH) from Bacillus megaterium IWG3 has been determined to an R-factor of 17.9% at 1.7 A resolution. The enzyme consists of four identical subunits, which are similar to those of other short-chain reductases/dehydrogenases (SDRs) in their overall folding and subunit architecture, although cofactor binding sites and subunit interactions differ. Whereas a pair of basic residues is well conserved among NADP(+)-preferring SDRs, only Arg39 was found around the adenine ribose moiety of GlcDH. This suggests that one basic amino acid is enough to determine the coenzyme specificity. The four subunits are interrelated by three mutually perpendicular diad axes (P, Q, and R). While subunit interactions through the P-axis for GlcDH are not so different from those of the other SDRs, those through the Q-axis differ significantly. GlcDH was found to have weaker hydrophobic interactions in the Q-interface. Moreover, GlcDH lacks the salt bridge that stabilizes the subunit interaction in the Q-interface in the other SDRs. Hydrogen bonds between Q-axis related subunits are also less common than in the other SDRs. The GlcDH tetramer dissociates into inactive monomers at pH 9.0, which can be attributed mainly to the weakness of the Q-axis interface.

PubMed: 11173533
DOI: 10.1093/oxfordjournals.jbchem.a002858

Experimental method

X-RAY DIFFRACTION (1.7 Å)