1gpe
From Proteopedia
(New page: 200px<br /> <applet load="1gpe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gpe, resolution 1.8Å" /> '''GLUCOSE OXIDASE FROM...) |
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| - | [[Image:1gpe.gif|left|200px]]<br /> | + | [[Image:1gpe.gif|left|200px]]<br /><applet load="1gpe" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1gpe" size=" | + | |
caption="1gpe, resolution 1.8Å" /> | caption="1gpe, resolution 1.8Å" /> | ||
'''GLUCOSE OXIDASE FROM PENICILLIUM AMAGASAKIENSE'''<br /> | '''GLUCOSE OXIDASE FROM PENICILLIUM AMAGASAKIENSE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Glucose oxidase is a flavin-dependent enzyme which catalyses the oxidation | + | 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== | ==About this Structure== | ||
| - | 1GPE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_amagasakiense Penicillium amagasakiense] with NAG and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. 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]]. Active as [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] Full crystallographic information is available from [http:// | + | 1GPE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_amagasakiense Penicillium amagasakiense] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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]]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Penicillium amagasakiense]] | [[Category: Penicillium amagasakiense]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hecht, H | + | [[Category: Hecht, H J.]] |
[[Category: Hendle, J.]] | [[Category: Hendle, J.]] | ||
| - | [[Category: Kalisz, H | + | [[Category: Kalisz, H M.]] |
[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: oxidoreductase(flavoprotein)]] | [[Category: oxidoreductase(flavoprotein)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:33 2008'' |
Revision as of 10:52, 21 February 2008
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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 with and as ligands. The following page contains interesting information on the relation of 1GPE with [Glucose Oxidase]. Active as Glucose oxidase, with EC number 1.1.3.4 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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