6xiz: Difference between revisions

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 <StructureSection load='6xiz' size='340' side='right'caption='[[6xiz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6xiz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"pediococcus_lindneri"_henneberg_1926 "pediococcus lindneri" henneberg 1926]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XIZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6xiz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pediococcus_acidilactici Pediococcus acidilactici]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XIZ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6vow|6vow]], [[6vox|6vox]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <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">BTW26_06860, FEZ49_06610 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1254 "Pediococcus lindneri" Henneberg 1926])</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=6xiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xiz OCA], [https://pdbe.org/6xiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xiz RCSB], [https://www.ebi.ac.uk/pdbsum/6xiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xiz ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/A0A1A5VCP7_PEDAC A0A1A5VCP7_PEDAC]
-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>
+==See Also==
+*[[Laccase 3D structures|Laccase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6xiz" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Pediococcus lindneri henneberg 1926]]
 [[Category: Large Structures]]
-[[Category: Coler, E A]]
+[[Category: Pediococcus acidilactici]]
-[[Category: Collins, R]]
+[[Category: Coler EA]]
-[[Category: Pardo, I]]
+[[Category: Collins R]]
-[[Category: Partowmah, S H]]
+[[Category: Pardo I]]
-[[Category: Soares, A S]]
+[[Category: Partowmah SH]]
-[[Category: Acoustic droplet ejection]]
+[[Category: Soares AS]]
-[[Category: Combinatorial crystallization]]
-[[Category: Copper oxidase]]
-[[Category: Laccase]]
-[[Category: Lignin]]
-[[Category: Oxidoreductase]]