2mmz
From Proteopedia
(Difference between revisions)
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| - | + | ==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=''> | |
| - | + | == Structural highlights == | |
| - | ==Disease== | + | <table><tr><td colspan='2'>[[2mmz]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MMZ FirstGlance]. <br> |
| + | </td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLRX5, C14orf87 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mmz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mmz RCSB], [http://www.ebi.ac.uk/pdbsum/2mmz PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Disease == | ||
[[http://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. | [[http://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 == | ||
| + | [[http://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;"> | ||
| + | == 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<ref>PMID:24733926</ref> | |
| - | [ | + | |
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | [[ | + | </div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Banci, L.]] | [[Category: Banci, L.]] | ||
[[Category: Brancaccio, D.]] | [[Category: Brancaccio, D.]] | ||
Revision as of 06:53, 21 May 2014
Solution structure of the apo form of human glutaredoxin 5
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