2l4d: Difference between revisions
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==cytochrome c domain of pp3183 protein from Pseudomonas putida== | ==cytochrome c domain of pp3183 protein from Pseudomonas putida== | ||
<StructureSection load='2l4d' size='340' side='right'caption='[[2l4d | <StructureSection load='2l4d' size='340' side='right'caption='[[2l4d]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2l4d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2l4d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_KT2440 Pseudomonas putida KT2440]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L4D FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</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=2l4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l4d OCA], [https://pdbe.org/2l4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l4d RCSB], [https://www.ebi.ac.uk/pdbsum/2l4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l4d ProSAT]</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=2l4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l4d OCA], [https://pdbe.org/2l4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l4d RCSB], [https://www.ebi.ac.uk/pdbsum/2l4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l4d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q88I19_PSEPK Q88I19_PSEPK] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas putida KT2440]] | ||
[[Category: Banci | [[Category: Banci L]] | ||
[[Category: Bertini | [[Category: Bertini I]] | ||
[[Category: Ciofi-Baffoni | [[Category: Ciofi-Baffoni S]] | ||
[[Category: Kozyreva | [[Category: Kozyreva T]] | ||
[[Category: Mori | [[Category: Mori M]] | ||
[[Category: Wang | [[Category: Wang S]] | ||
Latest revision as of 12:16, 6 November 2024
cytochrome c domain of pp3183 protein from Pseudomonas putidacytochrome c domain of pp3183 protein from Pseudomonas putida
Structural highlights
FunctionPublication Abstract from PubMedSco proteins are widespread in eukaryotic and in many prokaryotic organisms. They have a thioredoxin-like fold and bind a single copper(I) or copper(II) ion through a CXXXC motif and a conserved His ligand, with both tight and weak affinities. They have been implicated in the assembly of the Cu(A) site of cytochrome c oxidase as copper chaperones and/or thioredoxins. In this work we have structurally characterized a Sco domain which is naturally fused with a typical electron transfer molecule, i.e., cytochrome c, in Pseudomonas putida. The thioredoxin-like Sco domain does not bind copper(II), binds copper(I) with weak affinity without involving the conserved His, and has redox properties consisting of a thioredoxin activity and of the ability of reducing copper(II) to copper(I), and iron(III) to iron(II) of the cytochrome c domain. These findings indicate that the His ligand coordination is the discriminating factor for introducing a metallochaperone function in a thioredoxin-like fold, typically responsible for electron transfer processes. A comparative structural analysis of the Sco domain from P. putida versus eukaryotic Sco proteins revealed structural determinants affecting the formation of a tight-affinity versus a weak-affinity copper binding site in Sco proteins. Sco proteins are involved in electron transfer processes.,Banci L, Bertini I, Ciofi-Baffoni S, Kozyreva T, Mori M, Wang S J Biol Inorg Chem. 2010 Dec 23. PMID:21181421[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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