4czo: Difference between revisions
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==Crystal structure of the extralong fungal manganese peroxidase from Ceriporiopsis subvermispora in complex with manganese== | ==Crystal structure of the extralong fungal manganese peroxidase from Ceriporiopsis subvermispora in complex with manganese== | ||
<StructureSection load='4czo' size='340' side='right' caption='[[4czo]], [[Resolution|resolution]] 1.20Å' scene=''> | <StructureSection load='4czo' size='340' side='right' caption='[[4czo]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4czn|4czn]], [[4czp|4czp]], [[4czq|4czq]], [[4czr|4czr]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4czn|4czn]], [[4czp|4czp]], [[4czq|4czq]], [[4czr|4czr]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Manganese_peroxidase Manganese peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.13 1.11.1.13] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Manganese_peroxidase Manganese peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.13 1.11.1.13] </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=4czo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4czo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4czo RCSB], [http://www.ebi.ac.uk/pdbsum/4czo 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=4czo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4czo OCA], [http://pdbe.org/4czo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4czo RCSB], [http://www.ebi.ac.uk/pdbsum/4czo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4czo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4czo" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Manganese peroxidase|Manganese peroxidase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:05, 5 August 2016
Crystal structure of the extralong fungal manganese peroxidase from Ceriporiopsis subvermispora in complex with manganeseCrystal structure of the extralong fungal manganese peroxidase from Ceriporiopsis subvermispora in complex with manganese
Structural highlights
Publication Abstract from PubMedThe genome of Ceriporiopsis subvermispora includes 13 manganese peroxidase (MnP) genes representative of the three subfamilies described in ligninolytic fungi, which share an Mn(2+)-oxidation site and have varying lengths of the C-terminal tail. Short, long and extralong MnPs were heterologously expressed and biochemically characterized, and the first structure of an extralong MnP was solved. Its C-terminal tail surrounds the haem-propionate access channel, contributing to Mn(2+) oxidation by the internal propionate, but prevents the oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS), which is only oxidized by short MnPs and by shortened-tail variants from site-directed mutagenesis. The tail, which is anchored by numerous contacts, not only affects the catalytic properties of long/extralong MnPs but is also associated with their high acidic stability. Cd(2+) binds at the Mn(2+)-oxidation site and competitively inhibits oxidation of both Mn(2+) and ABTS. Moreover, mutations blocking the haem-propionate channel prevent substrate oxidation. This agrees with molecular simulations that position ABTS at an electron-transfer distance from the haem propionates of an in silico shortened-tail form, while it cannot reach this position in the extralong MnP crystal structure. Only small differences exist between the long and the extralong MnPs, which do not justify their classification as two different subfamilies, but they significantly differ from the short MnPs, with the presence/absence of the C-terminal tail extension being implicated in these differences. Structural implications of the C-terminal tail in the catalytic and stability properties of manganese peroxidases from ligninolytic fungi.,Fernandez-Fueyo E, Acebes S, Ruiz-Duenas FJ, Martinez MJ, Romero A, Medrano FJ, Guallar V, Martinez AT Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3253-65. doi:, 10.1107/S1399004714022755. Epub 2014 Nov 22. PMID:25478843[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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