1k3i

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[[Image:1k3i.jpg|left|200px]]<br /><applet load="1k3i" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1k3i, resolution 1.40&Aring;" />
 
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'''Crystal Structure of the Precursor of Galactose Oxidase'''<br />
 
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==Overview==
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==Crystal Structure of the Precursor of Galactose Oxidase==
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<StructureSection load='1k3i' size='340' side='right'caption='[[1k3i]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1k3i]] 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=1K3I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K3I FirstGlance]. <br>
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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]] 1.4&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr>
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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=1k3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k3i OCA], [https://pdbe.org/1k3i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k3i RCSB], [https://www.ebi.ac.uk/pdbsum/1k3i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k3i 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/k3/1k3i_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=1k3i 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 ==
Galactose oxidase (EC ) is a monomeric enzyme that contains a single copper ion and catalyses the stereospecific oxidation of primary alcohols to their corresponding aldehydes. The protein contains an unusual covalent thioether bond between a tyrosine, which acts as a radical center during the two-electron reaction, and a cysteine. The enzyme is produced in a precursor form lacking the thioether bond and also possessing an additional 17-aa pro-sequence at the N terminus. Previous work has shown that the aerobic addition of Cu(2+) to the precursor is sufficient to generate fully processed mature enzyme. The structure of the precursor protein has been determined to 1.4 A, revealing the location of the pro-sequence and identifying structural differences between the precursor and the mature protein. Structural alignment of the precursor and mature forms of galactose oxidase shows that five regions of main chain and some key residues of the active site differ significantly between the two forms. The precursor structure provides a starting point for modeling the chemistry of thioether bond formation and pro-sequence cleavage.
Galactose oxidase (EC ) is a monomeric enzyme that contains a single copper ion and catalyses the stereospecific oxidation of primary alcohols to their corresponding aldehydes. The protein contains an unusual covalent thioether bond between a tyrosine, which acts as a radical center during the two-electron reaction, and a cysteine. The enzyme is produced in a precursor form lacking the thioether bond and also possessing an additional 17-aa pro-sequence at the N terminus. Previous work has shown that the aerobic addition of Cu(2+) to the precursor is sufficient to generate fully processed mature enzyme. The structure of the precursor protein has been determined to 1.4 A, revealing the location of the pro-sequence and identifying structural differences between the precursor and the mature protein. Structural alignment of the precursor and mature forms of galactose oxidase shows that five regions of main chain and some key residues of the active site differ significantly between the two forms. The precursor structure provides a starting point for modeling the chemistry of thioether bond formation and pro-sequence cleavage.
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==About this Structure==
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Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme.,Firbank SJ, Rogers MS, Wilmot CM, Dooley DM, Halcrow MA, Knowles PF, McPherson MJ, Phillips SE Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):12932-7. PMID:11698678<ref>PMID:11698678</ref>
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1K3I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_sp. Fusarium sp.] with <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Galactose_oxidase Galactose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.9 1.1.3.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3I OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme., Firbank SJ, Rogers MS, Wilmot CM, Dooley DM, Halcrow MA, Knowles PF, McPherson MJ, Phillips SE, Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):12932-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11698678 11698678]
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</div>
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[[Category: Fusarium sp.]]
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<div class="pdbe-citations 1k3i" style="background-color:#fffaf0;"></div>
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[[Category: Galactose oxidase]]
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[[Category: Single protein]]
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[[Category: Dooley, D M.]]
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[[Category: Firbank, S J.]]
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[[Category: Halcrow, M A.]]
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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: Rogers, M S.]]
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[[Category: Wilmot, C M.]]
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[[Category: ACT]]
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[[Category: CA]]
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[[Category: GLC]]
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[[Category: 7 blade beta propeller]]
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[[Category: precursor of copper enzyme.]]
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[[Category: prosequence form]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:46 2008''
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==See Also==
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*[[Galactose oxidase|Galactose oxidase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Fusarium sp]]
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[[Category: Large Structures]]
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[[Category: Dooley DM]]
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[[Category: Firbank SJ]]
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[[Category: Halcrow MA]]
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[[Category: Knowles PF]]
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[[Category: McPherson MJ]]
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[[Category: Phillips SEV]]
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[[Category: Rogers MS]]
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[[Category: Wilmot CM]]

Current revision

Crystal Structure of the Precursor of Galactose Oxidase

PDB ID 1k3i

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