4a2d: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a2d]] is a 1 chain structure with sequence from [http://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=2ve0 2ve0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A2D FirstGlance]. <br> | <table><tr><td colspan='2'>[[4a2d]] is a 1 chain structure with sequence from [http://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=2ve0 2ve0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A2D FirstGlance]. <br> | ||
</td></tr><tr><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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>< | </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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a2h|4a2h]], [[4a2e|4a2e]], [[4a2g|4a2g]], [[4a2f|4a2f]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a2h|4a2h]], [[4a2e|4a2e]], [[4a2g|4a2g]], [[4a2f|4a2f]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Laccase Laccase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Laccase Laccase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a2d RCSB], [http://www.ebi.ac.uk/pdbsum/4a2d PDBsum]</span></td></tr> | <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=4a2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a2d RCSB], [http://www.ebi.ac.uk/pdbsum/4a2d PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Coriolopsis gallica]] | [[Category: Coriolopsis gallica]] | ||
[[Category: Laccase]] | [[Category: Laccase]] | ||
[[Category: Horjales, E | [[Category: Horjales, E]] | ||
[[Category: Mora, E De La | [[Category: Mora, E De La]] | ||
[[Category: Rudino-Pinera, E | [[Category: Rudino-Pinera, E]] | ||
[[Category: Valderrama, B | [[Category: Valderrama, B]] | ||
[[Category: Blue multicopper oxidase]] | [[Category: Blue multicopper oxidase]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 12:52, 4 January 2015
CORIOLOPSIS GALLICA LACCASE T2 COPPER DEPLETED AT PH 4.5CORIOLOPSIS GALLICA LACCASE T2 COPPER DEPLETED AT PH 4.5
Structural highlights
Publication 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. References
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