2f6c
From Proteopedia
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|PDB= 2f6c |SIZE=350|CAPTION= <scene name='initialview01'>2f6c</scene>, resolution 1.84Å | |PDB= 2f6c |SIZE=350|CAPTION= <scene name='initialview01'>2f6c</scene>, resolution 1.84Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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, poxSG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204723 Peniophora sp. SG]) | |GENE= p2ox, poxSG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204723 Peniophora sp. SG]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1tzl|1TZL]], [[2f5v|2F5V]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f6c OCA], [http://www.ebi.ac.uk/pdbsum/2f6c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f6c RCSB]</span> | ||
}} | }} | ||
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[[Category: Heckmann-Pohl, D M.]] | [[Category: Heckmann-Pohl, D M.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: PEG]] | ||
| - | [[Category: PG4]] | ||
[[Category: covalent]] | [[Category: covalent]] | ||
[[Category: d2 tetramer]] | [[Category: d2 tetramer]] | ||
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[[Category: thermostability mutation]] | [[Category: thermostability mutation]] | ||
| - | ''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 02:58:33 2008'' |
Revision as of 23:58, 30 March 2008
| |||||||
| , resolution 1.84Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | p2ox, poxSG (Peniophora sp. SG) | ||||||
| Activity: | Pyranose oxidase, with EC number 1.1.3.10 | ||||||
| Related: | 1TZL, 2F5V
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Reaction geometry and thermostability of pyranose 2-oxidase from the white-rot fungus Peniophora sp., Thermostability mutant E542K
Overview
Pyranose 2-oxidase catalyzes the oxidation of a number of carbohydrates using dioxygen; glucose, for example, is oxidized at carbon 2. The structure of pyranose 2-oxidase with the reaction product 2-keto-beta-d-glucose bound in the active center is reported in a new crystal form at 1.41 A resolution. The binding structure suggests that the alpha-anomer cannot be processed. The binding mode of the oxidized product was used to model other sugars accepted by the enzyme and to explain its specificity and catalytic rates. The reported structure at pH 6.0 shows a drastic conformational change in the loop of residues 454-461 (loop 454-461) at the active center compared to that of a closely homologous enzyme analyzed at pH 4.5 with a bound acetate inhibitor. In our structures, the loop is highly mobile and shifts to make way for the sugar to pass into the active center. Presumably, loop 454-461 functions as a gatekeeper. Apart from the wild-type enzyme, a thermostable variant was analyzed at 1.84 A resolution. In this variant, Glu542 is exchanged for a lysine. The observed stabilization could be a result of the mutated residue changing an ionic contact at a comparatively weak interface of the tetramer.
About this Structure
2F6C is a Single protein structure of sequence from Peniophora sp. sg. Full crystallographic information is available from OCA.
Reference
Reaction geometry and thermostable variant of pyranose 2-oxidase from the white-rot fungus Peniophora sp., Bannwarth M, Heckmann-Pohl D, Bastian S, Giffhorn F, Schulz GE, Biochemistry. 2006 May 30;45(21):6587-95. PMID:16716069
Page seeded by OCA on Mon Mar 31 02:58:33 2008
Categories: Peniophora sp. sg | Pyranose oxidase | Single protein | Bannwarth, M. | Bastian, S. | Giffhorn, F. | Heckmann-Pohl, D M. | Schulz, G E. | Covalent | D2 tetramer | Flavoprotein | Glutathione-reductase related fold | Gmc oxidoreductase | Histidine-bound | Lignin degradation | Phbh fold | Thermostability mutation
