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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2l4d' size='340' side='right' caption='[[2l4d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PP3183, PP_3183 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160488 PSEPK])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PP3183, PP_3183 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160488 PSEPK])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l4d OCA], [http://pdbe.org/2l4d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l4d RCSB], [http://www.ebi.ac.uk/pdbsum/2l4d PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l4d OCA], [http://pdbe.org/2l4d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l4d RCSB], [http://www.ebi.ac.uk/pdbsum/2l4d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l4d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 22:32, 1 August 2018
cytochrome c domain of pp3183 protein from Pseudomonas putidacytochrome c domain of pp3183 protein from Pseudomonas putida
Structural highlights
Publication 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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