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New page: left|200px<br /><applet load="2igo" size="350" color="white" frame="true" align="right" spinBox="true" caption="2igo, resolution 1.95Å" /> '''Crystal structure of...
 
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[[Image:2igo.gif|left|200px]]<br /><applet load="2igo" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2igo, resolution 1.95&Aring;" />
'''Crystal structure of pyranose 2-oxidase H167A mutant with 2-fluoro-2-deoxy-D-glucose'''<br />


==Overview==
==Crystal structure of pyranose 2-oxidase H167A mutant with 2-fluoro-2-deoxy-D-glucose==
Pyranose 2-oxidase (P2Ox) participates in fungal lignin degradation by, producing the H2O2 needed for lignin-degrading peroxidases. The enzyme, oxidizes cellulose- and hemicellulose-derived aldopyranoses at C2, preferentially, but also on C3, to the corresponding ketoaldoses. To, investigate the structural determinants of catalysis, covalent, flavinylation, substrate binding, and regioselectivity, wild-type and, mutant P2Ox enzymes were produced and characterized biochemically and, structurally. Removal of the histidyl-FAD linkage resulted in a, catalytically competent enzyme containing tightly, but noncovalently bound, FAD. This mutant (H167A) is characterized by a 5-fold lower kcat, and a, 35-mV lower redox potential, although no significant structural changes, were seen in its crystal structure. In previous structures of P2Ox, the, substrate loop (residues 452-457) covering the active site has been either, disordered or in a conformation incompatible with carbohydrate binding. We, present here the crystal structure of H167A in complex with a slow, substrate, 2-fluoro-2-deoxy-D-glucose. Based on the details of, 2-fluoro-2-deoxy-D-glucose binding in position for oxidation at C3, we, also outline a probable binding mode for D-glucose positioned for, regioselective oxidation at C2. The tentative determinant for, discriminating between the two binding modes is the position of the O6, hydroxyl group, which in the C2-oxidation mode can make favorable, interactions with Asp452 in the substrate loop and, possibly, a nearby, arginine residue (Arg472). We also substantiate our hypothesis with, steady-state kinetics data for the alanine replacements of Asp452 and, Arg472 as well as the double alanine 452/472 mutant.
<StructureSection load='2igo' size='340' side='right'caption='[[2igo]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2igo]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Trametes_ochracea Trametes ochracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IGO 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]] 1.95&#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=SHG:2-DEOXY-2-FLUORO-BETA-D-GLUCOPYRANOSE'>SHG</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=2igo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2igo OCA], [https://pdbe.org/2igo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2igo RCSB], [https://www.ebi.ac.uk/pdbsum/2igo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2igo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7ZA32_TRAOC Q7ZA32_TRAOC]
== 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/ig/2igo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2igo ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2IGO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trametes_ochracea Trametes ochracea] with <scene name='pdbligand=G2F:'>G2F</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IGO OCA].
*[[Pyranose oxidase|Pyranose oxidase]]
 
__TOC__
==Reference==
</StructureSection>
Structural basis for substrate binding and regioselective oxidation of monosaccharides at C3 by pyranose 2-oxidase., Kujawa M, Ebner H, Leitner C, Hallberg BM, Prongjit M, Sucharitakul J, Ludwig R, Rudsander U, Peterbauer C, Chaiyen P, Haltrich D, Divne C, J Biol Chem. 2006 Nov 17;281(46):35104-15. Epub 2006 Sep 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16984920 16984920]
[[Category: Large Structures]]
[[Category: Pyranose oxidase]]
[[Category: Single protein]]
[[Category: Trametes ochracea]]
[[Category: Trametes ochracea]]
[[Category: Divne, C.]]
[[Category: Divne C]]
[[Category: FAD]]
[[Category: G2F]]
[[Category: 2-fluoro-2-deoxy-d-glucose]]
[[Category: 8-alpha-(n3) histidyl flavinylation]]
[[Category: gmc oxidoreductase]]
[[Category: h167a mutant]]
[[Category: homotetramer]]
[[Category: oxidoreductase]]
[[Category: phbh fold]]
[[Category: rossman fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:40:36 2008''

Latest revision as of 09:03, 21 February 2024

Crystal structure of pyranose 2-oxidase H167A mutant with 2-fluoro-2-deoxy-D-glucose

2igo, resolution 1.95Å

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