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| | ==Solution structure of the apo form of human glutaredoxin 5== | | ==Solution structure of the apo form of human glutaredoxin 5== |
| - | <StructureSection load='2mmz' size='340' side='right'caption='[[2mmz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2mmz' size='340' side='right'caption='[[2mmz]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mmz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MMZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mmz]] is a 1 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=2MMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MMZ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLRX5, C14orf87 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </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=2mmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mmz OCA], [https://pdbe.org/2mmz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mmz RCSB], [https://www.ebi.ac.uk/pdbsum/2mmz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mmz 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=2mmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mmz OCA], [https://pdbe.org/2mmz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mmz RCSB], [https://www.ebi.ac.uk/pdbsum/2mmz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mmz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/GLRX5_HUMAN GLRX5_HUMAN]] Adult-onset autosomal recessive sideroblastic anemia. The disease is caused by mutations affecting the gene represented in this entry.
| + | [https://www.uniprot.org/uniprot/GLRX5_HUMAN GLRX5_HUMAN] Adult-onset autosomal recessive sideroblastic anemia. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GLRX5_HUMAN GLRX5_HUMAN]] Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. Required for normal iron homeostasis. Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1.
| + | [https://www.uniprot.org/uniprot/GLRX5_HUMAN GLRX5_HUMAN] Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. Required for normal iron homeostasis. Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Banci, L]] | + | [[Category: Banci L]] |
| - | [[Category: Brancaccio, D]] | + | [[Category: Brancaccio D]] |
| - | [[Category: Ciofi-Baffoni, S]] | + | [[Category: Ciofi-Baffoni S]] |
| - | [[Category: Conte, R Del]] | + | [[Category: Del Conte R]] |
| - | [[Category: Gadepalli, R]] | + | [[Category: Gadepalli R]] |
| - | [[Category: Mikolajczyk, M]] | + | [[Category: Mikolajczyk M]] |
| - | [[Category: Neri, S]] | + | [[Category: Neri S]] |
| - | [[Category: Piccioli, M]] | + | [[Category: Piccioli M]] |
| - | [[Category: Winkelmann, J]] | + | [[Category: Winkelmann J]] |
| - | [[Category: Iron-sulfur protein biogenesis]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Monothiol glutaredoxin]]
| + | |
| Structural highlights
Disease
GLRX5_HUMAN Adult-onset autosomal recessive sideroblastic anemia. The disease is caused by mutations affecting the gene represented in this entry.
Function
GLRX5_HUMAN Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. Required for normal iron homeostasis. Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1.
Publication Abstract from PubMed
Monothiol glutaredoxins play a crucial role in iron-sulfur (Fe/S) protein biogenesis. Essentially all of them can coordinate a [2Fe-2S] cluster and have been proposed to mediate the transfer of [2Fe-2S] clusters from scaffold proteins to target apo proteins, possibly by acting as cluster transfer proteins. The molecular basis of [2Fe-2S] cluster transfer from monothiol glutaredoxins to target proteins is a fundamental, but still unresolved, aspect to be defined in Fe/S protein biogenesis. In mitochondria monothiol glutaredoxin 5 (GRX5) is involved in the maturation of all cellular Fe/S proteins and participates in cellular iron regulation. Here we show that the structural plasticity of the dimeric state of the [2Fe-2S] bound form of human GRX5 (holo hGRX5) is the crucial factor that allows an efficient cluster transfer to the partner proteins human ISCA1 and ISCA2 by a specific protein-protein recognition mechanism. Holo hGRX5 works as a metallochaperone preventing the [2Fe-2S] cluster to be released in solution in the presence of physiological concentrations of glutathione and forming a transient, cluster-mediated protein-protein intermediate with two physiological protein partners receiving the [2Fe-2S] cluster. The cluster transfer mechanism defined here may extend to other mitochondrial [2Fe-2S] target proteins.
[2Fe-2S] cluster transfer in iron-sulfur protein biogenesis.,Banci L, Brancaccio D, Ciofi-Baffoni S, Del Conte R, Gadepalli R, Mikolajczyk M, Neri S, Piccioli M, Winkelmann J Proc Natl Acad Sci U S A. 2014 Apr 29;111(17):6203-8. doi:, 10.1073/pnas.1400102111. Epub 2014 Apr 14. PMID:24733926[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Banci L, Brancaccio D, Ciofi-Baffoni S, Del Conte R, Gadepalli R, Mikolajczyk M, Neri S, Piccioli M, Winkelmann J. [2Fe-2S] cluster transfer in iron-sulfur protein biogenesis. Proc Natl Acad Sci U S A. 2014 Apr 29;111(17):6203-8. doi:, 10.1073/pnas.1400102111. Epub 2014 Apr 14. PMID:24733926 doi:http://dx.doi.org/10.1073/pnas.1400102111
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