2f5v
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2f5v.gif|left|200px]] | [[Image:2f5v.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2f5v", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | + | {{STRUCTURE_2f5v| PDB=2f5v | SCENE= }} | |
- | + | ||
- | + | ||
- | }} | + | |
'''Reaction geometry and thermostability mutant of pyranose 2-oxidase from the white-rot fungus Peniophora sp.''' | '''Reaction geometry and thermostability mutant of pyranose 2-oxidase from the white-rot fungus Peniophora sp.''' | ||
Line 31: | Line 28: | ||
[[Category: Heckmann-Pohl, D.]] | [[Category: Heckmann-Pohl, D.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
- | [[Category: | + | [[Category: D2]] |
- | [[Category: | + | [[Category: Flavoprotein]] |
- | [[Category: | + | [[Category: Glutathion-reductase related fold]] |
- | [[Category: | + | [[Category: Gmc oxidoreductase]] |
- | [[Category: | + | [[Category: Phbh-fold]] |
- | [[Category: | + | [[Category: Rossmann-fold]] |
- | [[Category: | + | [[Category: Tetramer]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:29:44 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 00:29, 4 May 2008
Reaction geometry and thermostability mutant 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; 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
2F5V 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 Sun May 4 03:29:44 2008