1tzl
From Proteopedia
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|PDB= 1tzl |SIZE=350|CAPTION= <scene name='initialview01'>1tzl</scene>, resolution 2.35Å | |PDB= 1tzl |SIZE=350|CAPTION= <scene name='initialview01'>1tzl</scene>, resolution 2.35Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Pyranose_oxidase Pyranose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.10 1.1.3.10] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyranose_oxidase Pyranose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.10 1.1.3.10] </span> |
|GENE= p2ox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204723 Peniophora sp. SG]) | |GENE= p2ox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204723 Peniophora sp. SG]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tzl OCA], [http://www.ebi.ac.uk/pdbsum/1tzl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tzl RCSB]</span> | ||
}} | }} | ||
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[[Category: Heckmann-Pohl, D.]] | [[Category: Heckmann-Pohl, D.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: FAD]] | ||
[[Category: glucose-methanol-choline family]] | [[Category: glucose-methanol-choline family]] | ||
[[Category: gmc oxidoreductase]] | [[Category: gmc oxidoreductase]] | ||
[[Category: large inner cavity]] | [[Category: large inner cavity]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:03:19 2008'' |
Revision as of 21:03, 30 March 2008
| |||||||
| , resolution 2.35Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | p2ox (Peniophora sp. SG) | ||||||
| Activity: | Pyranose oxidase, with EC number 1.1.3.10 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Pyranose 2-Oxidase from the White-Rot Fungus Peniophora sp.
Overview
Pyranose 2-oxidase catalyzes the oxidation of a number of carbohydrates using dioxygen. The enzyme forms a D(2) symmetric homotetramer and contains one covalently bound FAD per subunit. The structure of the enzyme from Peniophora sp. was determined by multiwavelength anomalous diffraction (MAD) based on 96 selenium sites per crystallographic asymmetric unit and subsequently refined to good-quality indices. According to its chain fold, the enzyme belongs to the large glutathione reductase family and, in a more narrow sense, to the glucose-methanol-choline oxidoreductase (GMC) family. The tetramer contains a spacious central cavity from which the substrate enters one of the four active centers by penetrating a mobile barrier. Since this cavity can only be accessed by glucose-sized molecules, the enzyme does not convert sugars that are part of a larger molecule. The geometry of the active center and a comparison with an inhibitor complex of the homologous enzyme cellobiose dehydrogenase allow the modeling of the reaction at a high confidence level.
About this Structure
1TZL is a Single protein structure of sequence from Peniophora sp. sg. Full crystallographic information is available from OCA.
Reference
Crystal structure of pyranose 2-oxidase from the white-rot fungus Peniophora sp., Bannwarth M, Bastian S, Heckmann-Pohl D, Giffhorn F, Schulz GE, Biochemistry. 2004 Sep 21;43(37):11683-90. PMID:15362852
Page seeded by OCA on Mon Mar 31 00:03:19 2008
