1t2x

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{{Seed}}
 
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[[Image:1t2x.png|left|200px]]
 
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==Glactose oxidase C383S mutant identified by directed evolution==
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The line below this paragraph, containing "STRUCTURE_1t2x", creates the "Structure Box" on the page.
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<StructureSection load='1t2x' size='340' side='right'caption='[[1t2x]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1t2x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_sp. Fusarium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T2X FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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{{STRUCTURE_1t2x| PDB=1t2x | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t2x OCA], [https://pdbe.org/1t2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t2x RCSB], [https://www.ebi.ac.uk/pdbsum/1t2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t2x ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GAOA_GIBZA GAOA_GIBZA] Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides.<ref>PMID:13641238</ref> <ref>PMID:4441089</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t2/1t2x_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1t2x ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Galactose oxidase (GO; E.C. 1.1.3.9) is a copper- containing enzyme that oxidizes a range of primary alcohols to aldehydes. This broad substrate specificity is reflected in a high K(M) for substrates. Directed evolution has previously been used to select variants of GO that exhibit enhanced expression and kinetic properties. In assays using unpurified enzyme samples, the variant C383S displayed a 5-fold lower K(M) than wild-type GO. In the present study, we have constructed, expressed, purified and characterized a number of single, double and triple mutants at residues Cys383, Tyr436 and Val494, identified in one of the directed evolution studies, to examine their relative contributions to improved catalytic activity of GO. We report kinetic studies on the various mutant enzymes. In addition, we have determined the three-dimensional structure of the C383S variant. As with many mutations identified in directed evolution experiments, the availability of structural information does not provide a definitive answer to the reason for the improved K(M) in the C383S variant protein.
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===Glactose oxidase C383S mutant identified by directed evolution===
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Structural and kinetic studies of a series of mutants of galactose oxidase identified by directed evolution.,Wilkinson D, Akumanyi N, Hurtado-Guerrero R, Dawkes H, Knowles PF, Phillips SE, McPherson MJ Protein Eng Des Sel. 2004 Feb;17(2):141-8. Epub 2004 Jan 12. PMID:15047910<ref>PMID:15047910</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1t2x" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15047910}}, adds the Publication Abstract to the page
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*[[Galactose oxidase|Galactose oxidase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15047910 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15047910}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Fusarium sp]]
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1T2X is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_sp. Fusarium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T2X OCA].
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[[Category: Large Structures]]
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[[Category: Akumanyi N]]
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==Reference==
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[[Category: Dawkes H]]
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<ref group="xtra">PMID:15047910</ref><references group="xtra"/>
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[[Category: Hurtado-Guerrero R]]
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[[Category: Fusarium sp.]]
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[[Category: Knowles PF]]
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[[Category: Galactose oxidase]]
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[[Category: McPherson MJ]]
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[[Category: Akumanyi, N.]]
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[[Category: Phillips SEV]]
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[[Category: Dawkes, H.]]
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[[Category: Wilkinson D]]
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[[Category: Hurtado-Guerrero, R.]]
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[[Category: Knowles, P F.]]
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[[Category: McPherson, M J.]]
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[[Category: Phillips, S E.V.]]
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[[Category: Wilkinson, D.]]
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[[Category: 7 blade beta propeller]]
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[[Category: C383s mutant form]]
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[[Category: Mutant form of copper containing enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 14:33:07 2009''
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Current revision

Glactose oxidase C383S mutant identified by directed evolution

PDB ID 1t2x

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