5e9n: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Steccherinum murashkinskyi laccase at 0.95 resolution==
-<StructureSection load='5e9n' size='340' side='right' caption='[[5e9n]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
+<StructureSection load='5e9n' size='340' side='right'caption='[[5e9n]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5e9n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Steccherinum_murashkinskyi Steccherinum murashkinskyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E9N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E9N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5e9n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Steccherinum_murashkinskyi Steccherinum murashkinskyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E9N FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</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]] 0.95&#8491;</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 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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</scene></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=5e9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e9n OCA], [http://pdbe.org/5e9n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e9n RCSB], [http://www.ebi.ac.uk/pdbsum/5e9n PDBsum]</span></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=5e9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e9n OCA], [https://pdbe.org/5e9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e9n RCSB], [https://www.ebi.ac.uk/pdbsum/5e9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e9n ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/I1VE66_9APHY I1VE66_9APHY]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Laccases are multicopper oxidases that catalyze oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of dioxygen to water. The physicochemical and catalytic properties of two new fungal laccases from basidiomycetes Antrodiella faginea (AfL) and Steccherinum murashkinskyi (SmL) with middle redox potential of the T1 copper site were studied. The X-ray structures of AfL and SmL were solved at 1.75A and 0.95A, respectively. The oxidized state of copper ions in the active site was observed in AfL structure, while the mixture of oxidized and reduced states was observed in SmL structure. These oxidized and reduced states relate to the position of copper ions, their coordination, and nature and position of oxygen ligands. Comparative analysis of the T1 site environment of laccases with known structure allowed us to highlight the six types of the secondary coordination sphere of the T1 copper. The solvent accessible surface area of the conservative region of the secondary coordination sphere of the T1 copper correlates with its the redox potential. It was shown that the laccase classification by the structure of the T1 copper secondary coordination sphere is in agreement to ecophysiological behavior of laccase producing fungi.
+Structure-function study of two new middle-redox potential laccases from basidiomycetes Antrodiella faginea and Steccherinum murashkinskyi.,Glazunova OA, Polyakov KM, Moiseenko KV, Kurzeev SA, Fedorova TV Int J Biol Macromol. 2018 Jun 15;118(Pt A):406-418. doi:, 10.1016/j.ijbiomac.2018.06.038. PMID:29890251<ref>PMID:29890251</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5e9n" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Laccase 3D structures|Laccase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Laccase]]
+[[Category: Large Structures]]
 [[Category: Steccherinum murashkinskyi]]
-[[Category: Fedorova, T V]]
+[[Category: Fedorova TV]]
-[[Category: Glazunova, O A]]
+[[Category: Glazunova OA]]
-[[Category: Koroleva, O V]]
+[[Category: Koroleva OV]]
-[[Category: Polyakov, K M]]
+[[Category: Polyakov KM]]
-[[Category: Enzyme]]
-[[Category: Oxidoreductase]]