4a2e: Difference between revisions
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< | ==Crystal Structure of a Coriolopsis gallica Laccase at 1.7 A Resolution pH 5.5== | ||
<StructureSection load='4a2e' size='340' side='right'caption='[[4a2e]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4a2e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Coriolopsis_gallica Coriolopsis gallica]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2vdz 2vdz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A2E 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]] 1.8Å</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4a2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a2e OCA], [https://pdbe.org/4a2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a2e RCSB], [https://www.ebi.ac.uk/pdbsum/4a2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a2e ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q1W6B1_9APHY Q1W6B1_9APHY] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
X-ray radiation induces two main effects at metal centres contained in protein crystals: radiation-induced reduction and radiolysis and a resulting decrease in metal occupancy. In blue multicopper oxidases (BMCOs), the geometry of the active centres and the metal-to-ligand distances change depending on the oxidation states of the Cu atoms, suggesting that these alterations are catalytically relevant to the binding, activation and reduction of O(2). In this work, the X-ray-determined three-dimensional structure of laccase from the basidiomycete Coriolopsis gallica (Cg L), a high catalytic potential BMCO, is described. By combining spectroscopic techniques (UV-Vis, EPR and XAS) and X-ray crystallography, structural changes at and around the active copper centres were related to pH and absorbed X-ray dose (energy deposited per unit mass). Depletion of two of the four active Cu atoms as well as low occupancies of the remaining Cu atoms, together with different conformations of the metal centres, were observed at both acidic pH and high absorbed dose, correlating with more reduced states of the active coppers. These observations provide additional evidence to support the role of flexibility of copper sites during O(2) reduction. This study supports previous observations indicating that interpretations regarding redox state and metal coordination need to take radiation effects explicitly into account. | |||
Structural changes caused by radiation-induced reduction and radiolysis: the effect of X-ray absorbed dose in a fungal multicopper oxidase.,De la Mora E, Lovett JE, Blanford CF, Garman EF, Valderrama B, Rudino-Pinera E Acta Crystallogr D Biol Crystallogr. 2012 May;68(Pt 5):564-77. Epub 2012 Apr 17. PMID:22525754<ref>PMID:22525754</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4a2e" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Laccase 3D structures|Laccase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Coriolopsis gallica]] | [[Category: Coriolopsis gallica]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: De La Mora E]] | ||
[[Category: | [[Category: Horjales E]] | ||
[[Category: Rudino-Pinera | [[Category: Rudino-Pinera E]] | ||
[[Category: Valderrama | [[Category: Valderrama B]] | ||
Latest revision as of 14:18, 20 December 2023
Crystal Structure of a Coriolopsis gallica Laccase at 1.7 A Resolution pH 5.5Crystal Structure of a Coriolopsis gallica Laccase at 1.7 A Resolution pH 5.5
Structural highlights
FunctionPublication Abstract from PubMedX-ray radiation induces two main effects at metal centres contained in protein crystals: radiation-induced reduction and radiolysis and a resulting decrease in metal occupancy. In blue multicopper oxidases (BMCOs), the geometry of the active centres and the metal-to-ligand distances change depending on the oxidation states of the Cu atoms, suggesting that these alterations are catalytically relevant to the binding, activation and reduction of O(2). In this work, the X-ray-determined three-dimensional structure of laccase from the basidiomycete Coriolopsis gallica (Cg L), a high catalytic potential BMCO, is described. By combining spectroscopic techniques (UV-Vis, EPR and XAS) and X-ray crystallography, structural changes at and around the active copper centres were related to pH and absorbed X-ray dose (energy deposited per unit mass). Depletion of two of the four active Cu atoms as well as low occupancies of the remaining Cu atoms, together with different conformations of the metal centres, were observed at both acidic pH and high absorbed dose, correlating with more reduced states of the active coppers. These observations provide additional evidence to support the role of flexibility of copper sites during O(2) reduction. This study supports previous observations indicating that interpretations regarding redox state and metal coordination need to take radiation effects explicitly into account. Structural changes caused by radiation-induced reduction and radiolysis: the effect of X-ray absorbed dose in a fungal multicopper oxidase.,De la Mora E, Lovett JE, Blanford CF, Garman EF, Valderrama B, Rudino-Pinera E Acta Crystallogr D Biol Crystallogr. 2012 May;68(Pt 5):564-77. Epub 2012 Apr 17. PMID:22525754[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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