2l0y
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2l0y is ON HOLD Authors: Bertini, I., Ciofi-Baffoni, S., Gallo, A. Description: Complex hMia40-hCox17 ''Page seeded by [http://oca.weizmann.ac.il/...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Complex hMia40-hCox17== | |
| + | <StructureSection load='2l0y' size='340' side='right'caption='[[2l0y]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2l0y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L0Y FirstGlance]. <br> | ||
| + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0y OCA], [https://pdbe.org/2l0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l0y RCSB], [https://www.ebi.ac.uk/pdbsum/2l0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l0y ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Several proteins of the mitochondrial intermembrane space are targeted by internal targeting signals. A class of such proteins with alpha-helical hairpin structure bridged by two intramolecular disulfides is trapped by a Mia40-dependent oxidative process. Here, we describe the oxidative folding mechanism underpinning this process by an exhaustive structural characterization of the protein in all stages and as a complex with Mia40. Two consecutive induced folding steps are at the basis of the protein-trapping process. In the first one, Mia40 functions as a molecular chaperone assisting alpha-helical folding of the internal targeting signal of the substrate. Subsequently, in a Mia40-independent manner, folding of the second substrate helix is induced by the folded targeting signal functioning as a folding scaffold. The Mia40-induced folding pathway provides a proof of principle for the general concept that internal targeting signals may operate as a folding nucleus upon compartment-specific activation. | ||
| - | + | Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import.,Banci L, Bertini I, Cefaro C, Cenacchi L, Ciofi-Baffoni S, Felli IC, Gallo A, Gonnelli L, Luchinat E, Sideris D, Tokatlidis K Proc Natl Acad Sci U S A. 2010 Nov 8. PMID:21059946<ref>PMID:21059946</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2l0y" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bertini I]] | ||
| + | [[Category: Ciofi-Baffoni S]] | ||
| + | [[Category: Gallo A]] | ||
Current revision
Complex hMia40-hCox17
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