View source for 2f5v


==Reaction geometry and thermostability mutant of pyranose 2-oxidase from the white-rot fungus Peniophora sp.==
<StructureSection load='2f5v' size='340' side='right'caption='[[2f5v]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2f5v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Peniophora_sp._SG Peniophora sp. SG]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F5V FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.41&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=KBG:2-KETO-BETA-D-GLUCOSE'>KBG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f5v OCA], [https://pdbe.org/2f5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f5v RCSB], [https://www.ebi.ac.uk/pdbsum/2f5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f5v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/P2OX_PENSG P2OX_PENSG] Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H(2)O(2) for the ligninolytic peroxidases, lignin peroxidase and manganese-dependent peroxidase (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f5/2f5v_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f5v ConSurf].
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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<ref>PMID:16716069</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2f5v" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pyranose oxidase|Pyranose oxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Peniophora sp. SG]]
[[Category: Bannwarth M]]
[[Category: Bastian S]]
[[Category: Giffhorn F]]
[[Category: Heckmann-Pohl D]]
[[Category: Schulz GE]]