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| | ==CRYSTAL STRUCTURE OF GLUCOSE DEHYDROGENASE COMPLEXED WITH NAD+== | | ==CRYSTAL STRUCTURE OF GLUCOSE DEHYDROGENASE COMPLEXED WITH NAD+== |
| - | <StructureSection load='1gco' size='340' side='right' caption='[[1gco]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='1gco' size='340' side='right'caption='[[1gco]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gco]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. The May 2006 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Glucose Oxidase'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2006_5 10.2210/rcsb_pdb/mom_2006_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GCO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gco]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. The May 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Glucose Oxidase'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_5 10.2210/rcsb_pdb/mom_2006_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GCO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose_1-dehydrogenase Glucose 1-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.47 1.1.1.47] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gco OCA], [http://pdbe.org/1gco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gco RCSB], [http://www.ebi.ac.uk/pdbsum/1gco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gco ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gco OCA], [https://pdbe.org/1gco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gco RCSB], [https://www.ebi.ac.uk/pdbsum/1gco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gco ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DHG_PRIMG DHG_PRIMG] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 14581]] | |
| - | [[Category: Glucose 1-dehydrogenase]] | |
| | [[Category: Glucose Oxidase]] | | [[Category: Glucose Oxidase]] |
| | + | [[Category: Large Structures]] |
| | + | [[Category: Priestia megaterium]] |
| | [[Category: RCSB PDB Molecule of the Month]] | | [[Category: RCSB PDB Molecule of the Month]] |
| - | [[Category: Kurisu, G]] | + | [[Category: Kurisu G]] |
| - | [[Category: Kusunoki, M]] | + | [[Category: Kusunoki M]] |
| - | [[Category: Osaki, S]] | + | [[Category: Osaki S]] |
| - | [[Category: Tabata, S]] | + | [[Category: Tabata S]] |
| - | [[Category: Urabe, I]] | + | [[Category: Urabe I]] |
| - | [[Category: Yamamoto, K]] | + | [[Category: Yamamoto K]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Short-chain dehydrogenase/reductase]]
| + | |
| Structural highlights
Function
DHG_PRIMG
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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. 2001 Feb;129(2):303-12. PMID:11173533[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2001 Feb;129(2):303-12. PMID:11173533
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