2f5v
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(New page: 200px<br /><applet load="2f5v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f5v, resolution 1.41Å" /> '''Reaction geometry an...)
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Revision as of 08:15, 21 November 2007
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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 with KBG, FAD, PG4 and PEG as ligands. Active as Pyranose oxidase, with EC number 1.1.3.10 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
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