2l0y: Difference between revisions
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== Structural highlights == | == 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> | <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</td></tr> | </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> | <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> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 09:09, 27 November 2024
Complex hMia40-hCox17Complex hMia40-hCox17
Structural highlights
Publication Abstract from PubMedSeveral 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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