View source for 2mmz


==Solution structure of the apo form of human glutaredoxin 5==
<StructureSection load='2mmz' size='340' side='right'caption='[[2mmz]]' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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>
== 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.
== 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.
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mmz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Banci L]]
[[Category: Brancaccio D]]
[[Category: Ciofi-Baffoni S]]
[[Category: Del Conte R]]
[[Category: Gadepalli R]]
[[Category: Mikolajczyk M]]
[[Category: Neri S]]
[[Category: Piccioli M]]
[[Category: Winkelmann J]]