6xj0
From Proteopedia
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==Crystal structure of multi-copper oxidase from Pediococcus pentosaceus== | ==Crystal structure of multi-copper oxidase from Pediococcus pentosaceus== | ||
| - | <StructureSection load='6xj0' size='340' side='right'caption='[[6xj0]]' scene=''> | + | <StructureSection load='6xj0' size='340' side='right'caption='[[6xj0]], [[Resolution|resolution]] 2.34Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XJ0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6xj0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"pediococcus_hennebergii"_sollied_1903 "pediococcus hennebergii" sollied 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XJ0 FirstGlance]. <br> |
| - | </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=6xj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xj0 OCA], [https://pdbe.org/6xj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xj0 RCSB], [https://www.ebi.ac.uk/pdbsum/6xj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xj0 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2O:CU-O-CU+LINKAGE'>C2O</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mco, NCTC8066_01952 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1255 "Pediococcus hennebergii" Sollied 1903])</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=6xj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xj0 OCA], [https://pdbe.org/6xj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xj0 RCSB], [https://www.ebi.ac.uk/pdbsum/6xj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xj0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Prokaryotic laccases are emergent biocatalysts. However, they have not been broadly found and characterized in bacterial organisms, especially in lactic acid bacteria. Recently, a prokaryotic laccase from the lactic acid bacterium Pediococcus acidilactici 5930, which can degrade biogenic amines, was discovered. Thus, our study aimed to shed light on laccases from lactic acid bacteria focusing on two Pediococcus laccases, P. acidilactici 5930 and Pediococcus pentosaceus 4816, which have provided valuable information on their biochemical activities on redox mediators and biogenic amines. Both laccases are able to oxidize canonical substrates as ABTS, ferrocyanide and 2,6-DMP, and non-conventional substrates as biogenic amines. With ABTS as a substrate, they prefer an acidic environment and show sigmoidal kinetic activity, and are rather thermostable. Moreover, this study has provided the first structural view of two lactic acid bacteria laccases, revealing new structural features not seen before in other well-studied laccases, but which seem characteristic for this group of bacteria. We believe that understanding the role of laccases in lactic acid bacteria will have an impact on their biotechnological applications and provide a framework for the development of engineered lactic acid bacteria with enhanced properties. | ||
| + | |||
| + | Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species.,Olmeda I, Casino P, Collins RE, Sendra R, Callejon S, Huesa J, Soares AS, Ferrer S, Pardo I Microb Biotechnol. 2021 Feb 26. doi: 10.1111/1751-7915.13751. PMID:33635570<ref>PMID:33635570</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6xj0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Pediococcus hennebergii sollied 1903]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Coler | + | [[Category: Coler, E A]] |
| - | [[Category: Collins R]] | + | [[Category: Collins, R]] |
| - | [[Category: Pardo I]] | + | [[Category: Pardo, I]] |
| - | [[Category: Partowmah | + | [[Category: Partowmah, S H]] |
| - | [[Category: Soares | + | [[Category: Soares, A S]] |
| + | [[Category: Acoustic droplet ejection]] | ||
| + | [[Category: Combinatorial crystallization]] | ||
| + | [[Category: Copper oxidase]] | ||
| + | [[Category: Laccase]] | ||
| + | [[Category: Lignin]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 09:36, 12 May 2021
Crystal structure of multi-copper oxidase from Pediococcus pentosaceus
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