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==Solution structures of apo Sco1 protein from Thermus Thermophilus== | |||
<StructureSection load='2k6v' size='340' side='right'caption='[[2k6v]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2k6v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K6V FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2k6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k6v OCA], [https://pdbe.org/2k6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k6v RCSB], [https://www.ebi.ac.uk/pdbsum/2k6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k6v ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5SGY8_THET8 Q5SGY8_THET8] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/2k6v_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2k6v ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Copper is essential for proper functioning of cytochrome c oxidases, and therefore for cellular respiration in eukaryotes and many bacteria. Here we show that a new periplasmic protein (PCu(A)C) selectively inserts Cu(I) ions into subunit II of Thermus thermophilus ba(3) oxidase to generate a native Cu(A) site. The purported metallochaperone Sco1 is unable to deliver copper ions; instead, it works as a thiol-disulfide reductase to maintain the correct oxidation state of the Cu(A) cysteine ligands. | |||
Mechanism of Cu(A) assembly.,Abriata LA, Banci L, Bertini I, Ciofi-Baffoni S, Gkazonis P, Spyroulias GA, Vila AJ, Wang S Nat Chem Biol. 2008 Oct;4(10):599-601. Epub 2008 Aug 31. PMID:18758441<ref>PMID:18758441</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2k6v" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus HB8]] | |||
[[Category: Abriata LA]] | |||
[[Category: Banci L]] | |||
[[Category: Bertini I]] | |||
[[Category: Ciofi-Baffoni S]] | |||
[[Category: Gkazonis P]] | |||
[[Category: Spyroulias GA]] | |||
[[Category: Vila AJ]] | |||
[[Category: Wang S]] | |||
Latest revision as of 12:35, 22 May 2024
Solution structures of apo Sco1 protein from Thermus ThermophilusSolution structures of apo Sco1 protein from Thermus Thermophilus
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCopper is essential for proper functioning of cytochrome c oxidases, and therefore for cellular respiration in eukaryotes and many bacteria. Here we show that a new periplasmic protein (PCu(A)C) selectively inserts Cu(I) ions into subunit II of Thermus thermophilus ba(3) oxidase to generate a native Cu(A) site. The purported metallochaperone Sco1 is unable to deliver copper ions; instead, it works as a thiol-disulfide reductase to maintain the correct oxidation state of the Cu(A) cysteine ligands. Mechanism of Cu(A) assembly.,Abriata LA, Banci L, Bertini I, Ciofi-Baffoni S, Gkazonis P, Spyroulias GA, Vila AJ, Wang S Nat Chem Biol. 2008 Oct;4(10):599-601. Epub 2008 Aug 31. PMID:18758441[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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