6i3k

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<StructureSection load='6i3k' size='340' side='right'caption='[[6i3k]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='6i3k' size='340' side='right'caption='[[6i3k]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6i3k]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I3K FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6i3k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Albifimbria_verrucaria Albifimbria verrucaria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I3K FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
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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]] 1.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6i3j|6i3j]], [[6i3l|6i3l]]</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bilirubin_oxidase Bilirubin oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.5 1.3.3.5] </span></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=6i3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i3k OCA], [https://pdbe.org/6i3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i3k RCSB], [https://www.ebi.ac.uk/pdbsum/6i3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i3k ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6i3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i3k OCA], [http://pdbe.org/6i3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i3k RCSB], [http://www.ebi.ac.uk/pdbsum/6i3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i3k ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/BLRO_ALBVE BLRO_ALBVE]
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Unlike any protein studied so far, the active site of bilirubin oxidase from Myrothecium verrucaria contains a unique type of covalent link between tryptophan and histidine side chains. The role of this post-translational modification in substrate binding and oxidation is not sufficiently understood. Our structural and mutational studies provide evidence that this Trp396-His398 adduct modifies T1 copper coordination and is an important part of the substrate binding and oxidation site. The presence of the adduct is crucial for oxidation of substituted phenols and it substantially influences the rate of oxidation of bilirubin. Additionally, we bring the first structure of bilirubin oxidase in complex with one of its products, ferricyanide ion, interacting with the modified tryptophan side chain, Arg356 and the active site-forming loop 393-398. The results imply that structurally and chemically distinct types of substrates, including bilirubin, utilize the Trp-His adduct mainly for binding and to a smaller extent for electron transfer.
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Trp-His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer.,Koval T, Svecova L, Ostergaard LH, Skalova T, Duskova J, Hasek J, Kolenko P, Fejfarova K, Stransky J, Trundova M, Dohnalek J Sci Rep. 2019 Sep 23;9(1):13700. doi: 10.1038/s41598-019-50105-3. PMID:31548583<ref>PMID:31548583</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 6i3k" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bilirubin oxidase]]
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[[Category: Albifimbria verrucaria]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Dohnalek, J]]
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[[Category: Dohnalek J]]
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[[Category: Duskova, J]]
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[[Category: Duskova J]]
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[[Category: Kolenko, P]]
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[[Category: Kolenko P]]
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[[Category: Koval, T]]
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[[Category: Koval T]]
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[[Category: Ostergaard, L H]]
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[[Category: Ostergaard LH]]
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[[Category: Skalova, T]]
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[[Category: Skalova T]]
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[[Category: Svecova, L]]
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[[Category: Svecova L]]
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[[Category: Complex]]
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[[Category: Enzymatic activity]]
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[[Category: Mutant]]
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[[Category: Oxidoreductase]]
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Revision as of 07:35, 1 May 2024

Bilirubin oxidase from Myrothecium verrucaria, mutant W396A in complex with ferricyanide

PDB ID 6i3k

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