6l1v: Difference between revisions
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<StructureSection load='6l1v' size='340' side='right'caption='[[6l1v]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='6l1v' size='340' side='right'caption='[[6l1v]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6l1v]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L1V OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6l1v]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L1V 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></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]] 2.25Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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></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=6l1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l1v OCA], [https://pdbe.org/6l1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l1v RCSB], [https://www.ebi.ac.uk/pdbsum/6l1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l1v ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/AZUR1_ALCXX AZUR1_ALCXX] Transfers electrons from cytochrome c551 to cytochrome oxidase. | ||
<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 6l1v" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6l1v" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Azurin 3D structures|Azurin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Achromobacter xylosoxidans]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cahyono | [[Category: Cahyono RN]] | ||
[[Category: Higuchi | [[Category: Higuchi Y]] | ||
[[Category: Hirota | [[Category: Hirota S]] | ||
[[Category: Nagao | [[Category: Nagao S]] | ||
[[Category: Shibata | [[Category: Shibata N]] | ||
[[Category: Yamanaka | [[Category: Yamanaka M]] | ||
Latest revision as of 13:49, 22 November 2023
Domain-swapped Alcaligenes xylosoxidans azurin dimerDomain-swapped Alcaligenes xylosoxidans azurin dimer
Structural highlights
FunctionAZUR1_ALCXX Transfers electrons from cytochrome c551 to cytochrome oxidase. Publication Abstract from PubMedProtein oligomers have gained interest, owing to their increased knowledge in cells and promising utilization for future materials. Various proteins have been shown to 3D domain swap, but there has been no domain swapping report on a blue copper protein. Here, we found that azurin from Alcaligenes xylosoxidans oligomerizes by the procedure of 2,2,2-trifluoroethanol addition to Cu(i)-azurin at pH 5.0, lyophilization, and dissolution at pH 7.0, whereas it slightly oligomerizes when using Cu(ii)-azurin. The amount of high order oligomers increased with the addition of Cu(ii) ions to the dissolution process of a similar procedure for apoazurin, indicating that Cu(ii) ions enhance azurin oligomerization. The ratio of the absorbance at 460 nm to that at approximately 620 nm of the azurin dimer (Abs460/Abs618 = 0.113) was higher than that of the monomer (Abs460/Abs622 = 0.067) and the EPR A || value of the dimer (5.85 mT) was slightly smaller than that of the monomer (5.95 mT), indicating a slightly more rhombic copper coordination for the dimer. The redox potential of the azurin dimer was 342 +/- 5 mV vs. NHE, which was 50 mV higher than that of the monomer. According to X-ray crystal analysis, the azurin dimer exhibited a domain-swapped structure, where the N-terminal region containing three beta-strands was exchanged between protomers. The copper coordination structure was tetrahedrally distorted in the azurin dimer, similar to that in the monomer; however, the Cu-O(Gly45) bond length was longer for the dimer (monomer, 2.46-2.59 A; dimer, 2.98-3.25 A). These results open the door for designing oligomers of blue copper proteins by domain swapping. 3D domain swapping of azurin from Alcaligenes xylosoxidans.,Cahyono RN, Yamanaka M, Nagao S, Shibata N, Higuchi Y, Hirota S Metallomics. 2020 Jan 20. doi: 10.1039/c9mt00255c. PMID:31956880[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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