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| | ==Oxidized Yeast Adrenodoxin Homolog 1== | | ==Oxidized Yeast Adrenodoxin Homolog 1== |
| - | <StructureSection load='2mjd' size='340' side='right' caption='[[2mjd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2mjd' size='340' side='right'caption='[[2mjd]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mjd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MJD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mjd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MJD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mje|2mje]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YAH1, YPL252C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=2mjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mjd OCA], [https://pdbe.org/2mjd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mjd RCSB], [https://www.ebi.ac.uk/pdbsum/2mjd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mjd ProSAT]</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=2mjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mjd OCA], [http://pdbe.org/2mjd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mjd RCSB], [http://www.ebi.ac.uk/pdbsum/2mjd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mjd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ADRX_YEAST ADRX_YEAST]] Required for Fe-S cluster incorporation into mitochondrial and cytosolic apoproteins. May be part of a novel electron transport chain.<ref>PMID:10655482</ref> | + | [https://www.uniprot.org/uniprot/ADRX_YEAST ADRX_YEAST] Required for Fe-S cluster incorporation into mitochondrial and cytosolic apoproteins. May be part of a novel electron transport chain.<ref>PMID:10655482</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Ferredoxin|Ferredoxin]] | + | *[[Ferredoxin 3D structures|Ferredoxin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Banci, L]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Gallo, A]] | + | [[Category: Banci L]] |
| - | [[Category: 2fe2s cluster]] | + | [[Category: Gallo A]] |
| - | [[Category: Ferredoxin]]
| + | |
| - | [[Category: Iron sulfur assembly]]
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| - | [[Category: Metal binding protein]]
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| - | [[Category: Paramagnetic protein]]
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| Structural highlights
Function
ADRX_YEAST Required for Fe-S cluster incorporation into mitochondrial and cytosolic apoproteins. May be part of a novel electron transport chain.[1]
Publication Abstract from PubMed
Maturation of iron-sulphur (Fe/S) proteins involves complex biosynthetic machinery. In vivo synthesis of [2Fe-2S] clusters on the mitochondrial scaffold protein Isu1 requires the cysteine desulphurase complex Nfs1-Isd11, frataxin, ferredoxin Yah1 and its reductase Arh1. The roles of Yah1-Arh1 have remained enigmatic, because they are not required for in vitro Fe/S cluster assembly. Here, we reconstitute [2Fe-2S] cluster synthesis on Isu1 in a reaction depending on Nfs1-Isd11, frataxin, Yah1, Arh1 and NADPH. Unlike in the bacterial system, frataxin is an essential part of Fe/S cluster biosynthesis and is required simultaneously and stoichiometrically to Yah1. Reduced but not oxidized Yah1 tightly interacts with apo-Isu1 indicating a dynamic interaction between Yah1-apo-Isu1. Nuclear magnetic resonance structural studies identify the Yah1-apo-Isu1 interaction surface and suggest a pathway for electron flow from reduced ferredoxin to Isu1. Together, our study defines the molecular function of the ferredoxin Yah1 and its human orthologue FDX2 in mitochondrial Fe/S cluster synthesis.
Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin.,Webert H, Freibert SA, Gallo A, Heidenreich T, Linne U, Amlacher S, Hurt E, Muhlenhoff U, Banci L, Lill R Nat Commun. 2014 Oct 31;5:5013. doi: 10.1038/ncomms6013. PMID:25358379[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lange H, Kaut A, Kispal G, Lill R. A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins. Proc Natl Acad Sci U S A. 2000 Feb 1;97(3):1050-5. PMID:10655482
- ↑ Webert H, Freibert SA, Gallo A, Heidenreich T, Linne U, Amlacher S, Hurt E, Muhlenhoff U, Banci L, Lill R. Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin. Nat Commun. 2014 Oct 31;5:5013. doi: 10.1038/ncomms6013. PMID:25358379 doi:http://dx.doi.org/10.1038/ncomms6013
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