1gpe
From Proteopedia
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| - | [[Image:1gpe.gif|left|200px]] | + | [[Image:1gpe.gif|left|200px]] |
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| - | '''GLUCOSE OXIDASE FROM PENICILLIUM AMAGASAKIENSE''' | + | {{Structure |
| + | |PDB= 1gpe |SIZE=350|CAPTION= <scene name='initialview01'>1gpe</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Glucose_oxidase Glucose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.4 1.1.3.4] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''GLUCOSE OXIDASE FROM PENICILLIUM AMAGASAKIENSE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GPE is a [ | + | 1GPE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_amagasakiense Penicillium amagasakiense]. The following page contains interesting information on the relation of 1GPE with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb77_1.html Glucose Oxidase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPE OCA]. |
==Reference== | ==Reference== | ||
| - | 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes., Wohlfahrt G, Witt S, Hendle J, Schomburg D, Kalisz HM, Hecht HJ, Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):969-77. PMID:[http:// | + | 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes., Wohlfahrt G, Witt S, Hendle J, Schomburg D, Kalisz HM, Hecht HJ, Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):969-77. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10216293 10216293] |
[[Category: Glucose Oxidase]] | [[Category: Glucose Oxidase]] | ||
[[Category: Glucose oxidase]] | [[Category: Glucose oxidase]] | ||
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[[Category: oxidoreductase(flavoprotein)]] | [[Category: oxidoreductase(flavoprotein)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:26:13 2008'' |
Revision as of 09:26, 20 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Glucose oxidase, with EC number 1.1.3.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GLUCOSE OXIDASE FROM PENICILLIUM AMAGASAKIENSE
Overview
Glucose oxidase is a flavin-dependent enzyme which catalyses the oxidation of beta-D-glucose by molecular oxygen to delta-gluconolactone and hydrogen peroxide. The structure of the enzyme from Aspergillus niger, previously refined at 2.3 A resolution, has been refined at 1.9 A resolution to an R value of 19.0%, and the structure of the enzyme from Penicillium amagasakiense, which has 65% sequence identity, has been determined by molecular replacement and refined at 1.8 A resolution to an R value of 16.4%. The structures of the partially deglycosylated enzymes have an r.m.s. deviation of 0.7 A for main-chain atoms and show four N-glycosylation sites, with an extended carbohydrate moiety at Asn89. Substrate complexes of the enzyme from A. niger were modelled by force-field methods. The resulting model is consistent with results from site-directed mutagenesis experiments and shows the beta-D-glucose molecule in the active site of glucose oxidase, stabilized by 12 hydrogen bonds and by hydrophobic contacts to three neighbouring aromatic residues and to flavin adenine dinucleotide. Other hexoses, such as alpha-D-glucose, mannose and galactose, which are poor substrates for the enzyme, and 2-deoxy-D-glucose, form either fewer bonds or unfavourable contacts with neighbouring amino acids. Simulation of the complex between the reduced enzyme and the product, delta-gluconolactone, has provided an explanation for the lack of product inhibition by the lactone.
About this Structure
1GPE is a Single protein structure of sequence from Penicillium amagasakiense. The following page contains interesting information on the relation of 1GPE with [Glucose Oxidase]. Full crystallographic information is available from OCA.
Reference
1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes., Wohlfahrt G, Witt S, Hendle J, Schomburg D, Kalisz HM, Hecht HJ, Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):969-77. PMID:10216293
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