3t6z

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3t6z]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Steccherinum_ochraceum Steccherinum ochraceum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T6Z FirstGlance]. <br>
<table><tr><td colspan='2'>[[3t6z]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Steccherinum_ochraceum Steccherinum ochraceum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T6Z FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.15&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3t6v|3t6v]], [[3t6w|3t6w]], [[3t6x|3t6x]], [[3t71|3t71]]</div></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=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3t6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t6z OCA], [https://pdbe.org/3t6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t6z RCSB], [https://www.ebi.ac.uk/pdbsum/3t6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t6z ProSAT]</span></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=3t6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t6z OCA], [https://pdbe.org/3t6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t6z RCSB], [https://www.ebi.ac.uk/pdbsum/3t6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t6z ProSAT]</span></td></tr>
</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/I1SB14_9APHY I1SB14_9APHY]
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The crystal structure of a blue laccase from Steccherinum ochraceum has been solved at 2.0A of resolution using a classic data acquisition from a single crystal. The overall structural features are typical of this class of enzymes, however, distances inside the trinuclear copper cluster are indicative of a reduction of the metal centers induced by free electrons produced during the X-ray data collection. UV-visible spectra collected during the X-ray exposure support the progressive reduction of the metal centers. In order to better detect the reduction progression steps in the trinuclear copper site, a multicrystal data collection strategy based on a systematic spread of the X-ray dose over many crystals has been employed. This approach is based on collecting multicrystal data sets, then combining the slices of the individual data sets experiencing the same radiation dose to obtain composite complete data sets at progressively higher doses. Applying this technique, we have been able to capture sequential frames of the enzyme during the metal centers and molecular oxygen reduction mechanism obtaining a three-dimensional movie of the X-ray-driven catalytic conversion of the molecular oxygen in the active site of laccase: first, the copper ions reduction, then the molecular oxygen binding and its reductive splitting, thus allowing to reconstruct the entire catalytic cycle for multicopper oxidases.
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Reaction intermediates and redox state changes in a blue laccase from Steccherinum ochraceum observed by crystallographic high/low X-ray dose experiments.,Ferraroni M, Matera I, Chernykh A, Kolomytseva M, Golovleva LA, Scozzafava A, Briganti F J Inorg Biochem. 2012 Jan 31. PMID:22341982<ref>PMID:22341982</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 3t6z" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Laccase 3D structures|Laccase 3D structures]]
*[[Laccase 3D structures|Laccase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Steccherinum ochraceum]]
[[Category: Steccherinum ochraceum]]
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[[Category: Briganti, F]]
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[[Category: Briganti F]]
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[[Category: Chernykh, A M]]
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[[Category: Chernykh AM]]
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[[Category: Ferraroni, M]]
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[[Category: Ferraroni M]]
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[[Category: Golovleva, L]]
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[[Category: Golovleva L]]
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[[Category: Kolomytseva, M]]
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[[Category: Kolomytseva M]]
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[[Category: Matera, I]]
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[[Category: Matera I]]
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[[Category: Scozzafava, A]]
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[[Category: Scozzafava A]]
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[[Category: Beta barrel]]
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[[Category: Oxidoreductase]]
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Revision as of 13:19, 14 March 2024

Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose)

PDB ID 3t6z

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