1gco
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(New page: 200px<br /> <applet load="1gco" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gco, resolution 1.70Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 06:53, 18 November 2007
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CRYSTAL STRUCTURE OF GLUCOSE DEHYDROGENASE COMPLEXED WITH NAD+
Overview
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.
About this Structure
1GCO is a Single protein structure of sequence from Bacillus megaterium with NAD as ligand. The following page contains interesting information on the relation of 1GCO with [Glucose Oxidase]. Active as Glucose 1-dehydrogenase, with EC number 1.1.1.47 Full crystallographic information is available from OCA.
Reference
Crystal structure of glucose dehydrogenase from Bacillus megaterium IWG3 at 1.7 A resolution., Yamamoto K, Kurisu G, Kusunoki M, Tabata S, Urabe I, Osaki S, J Biochem (Tokyo). 2001 Feb;129(2):303-12. PMID:11173533
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