4e9x: Difference between revisions
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<StructureSection load='4e9x' size='340' side='right'caption='[[4e9x]], [[Resolution|resolution]] 1.14Å' scene=''> | <StructureSection load='4e9x' size='340' side='right'caption='[[4e9x]], [[Resolution|resolution]] 1.14Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4e9x]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4e9x]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E9X FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></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=4e9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9x OCA], [https://pdbe.org/4e9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e9x RCSB], [https://www.ebi.ac.uk/pdbsum/4e9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e9x ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/C0STU6_9BACT C0STU6_9BACT]] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4e9x" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4e9x" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Laccase 3D structures|Laccase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Uncultured bacterium]] | ||
[[Category: Higuchi | [[Category: Higuchi Y]] | ||
[[Category: Komori | [[Category: Komori H]] | ||
[[Category: Miyazaki | [[Category: Miyazaki K]] | ||
Revision as of 09:59, 28 September 2022
Multicopper Oxidase mgLAC (data3)Multicopper Oxidase mgLAC (data3)
Structural highlights
FunctionPublication Abstract from PubMedStructural models determined by X-ray crystallography play a central role in understanding the catalytic mechanism of enzymes. However, X-ray radiation generates hydrated electrons that can cause significant damage to the active sites of metalloenzymes. In the present study, crystal structures of the multicopper oxidases (MCOs) CueO from Escherichia coli and laccase from a metagenome were determined. Diffraction data were obtained from a single crystal under low to high X-ray dose conditions. At low levels of X-ray exposure, unambiguous electron density for an O atom was observed inside the trinuclear copper centre (TNC) in both MCOs. The gradual reduction of copper by hydrated electrons monitored by measurement of the Cu K-edge X-ray absorption spectra led to the disappearance of the electron density for the O atom. In addition, the size of the copper triangle was enlarged by a two-step shift in the location of the type III coppers owing to reduction. Further, binding of O2 to the TNC after its full reduction was observed in the case of the laccase. Based on these novel structural findings, the diverse resting structures of the MCOs and their four-electron O2-reduction process are discussed. New insights into the catalytic active-site structure of multicopper oxidases.,Komori H, Sugiyama R, Kataoka K, Miyazaki K, Higuchi Y, Sakurai T Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):772-9. doi:, 10.1107/S1399004713033051. Epub 2014 Feb 22. PMID:24598746[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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