4a67: Difference between revisions

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-[[Image:4a67.png|left|200px]]
-<!--
+==Mutations in the neighbourhood of CotA-laccase trinuclear site: D116E mutant==
-The line below this paragraph, containing "STRUCTURE_4a67", creates the "Structure Box" on the page.
+<StructureSection load='4a67' size='340' side='right'caption='[[4a67]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[4a67]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A67 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=PER:PEROXIDE+ION'>PER</scene></td></tr>
-{{STRUCTURE_4a67|  PDB=4a67  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a67 OCA], [https://pdbe.org/4a67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a67 RCSB], [https://www.ebi.ac.uk/pdbsum/4a67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a67 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/COTA_BACSU COTA_BACSU] Involved in brown pigmentation during sporogenesis.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Multi-copper oxidases constitute a family of proteins that are capable of coupling the one-electron oxidation of four substrate equivalents to the four-electron reduction of dioxygen to two molecules of water. The main catalytic stages occurring during the process have already been identified, but several questions remain, including the nature of the protonation events that take place during the reductive cleavage of dioxygen to water. The presence of a structurally conserved acidic residue (Glu498 in CotA laccase from Bacillus subtilis) at the dioxygen-entrance channel has been reported to play a decisive role in the protonation mechanisms, channelling protons during the reduction process and stabilizing the site as a whole. A second acidic residue that is sequentially conserved in multi-copper oxidases and sited within the exit channel (Asp116 in CotA) has also been identified as being important in the protonation process. In this study, CotA laccase has been used as a model system to assess the role of Asp116 in the reduction process of dioxygen to water. The crystal structures of three distinct mutants, D116E, D116N and D116A, produced by site-saturation mutagenesis have been determined. In addition, theoretical calculations have provided further support for a role of this residue in the protonation events.
-===Mutations in the neighbourhood of CotA-laccase trinuclear site: D116E mutant===
+The role of Asp116 in the reductive cleavage of dioxygen to water in CotA laccase: assistance during the proton-transfer mechanism.,Silva CS, Damas JM, Chen Z, Brissos V, Martins LO, Soares CM, Lindley PF, Bento I Acta Crystallogr D Biol Crystallogr. 2012 Feb;68(Pt 2):186-93. Epub 2012 Jan 17. PMID:22281748<ref>PMID:22281748</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4a67" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_22281748}}, adds the Publication Abstract to the page
+*[[Laccase 3D structures|Laccase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 22281748 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_22281748}}
+__TOC__
+</StructureSection>
-==About this Structure==
-[[4a67]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A67 OCA].
-==Reference==
-<ref group="xtra">PMID:022281748</ref><references group="xtra"/>
 [[Category: Bacillus subtilis]]
-[[Category: Laccase]]
+[[Category: Large Structures]]
-[[Category: Bento, I.]]
+[[Category: Bento I]]
-[[Category: Lindley, P F.]]
+[[Category: Lindley PF]]
-[[Category: Silva, C S.]]
+[[Category: Silva CS]]
-[[Category: Dioxygen reduction]]
-[[Category: Multi-copper oxidase]]
-[[Category: Oxidoreductase]]
-[[Category: Oxidoreductase activity]]
-[[Category: Trinuclear cluster]]