View source for 4pui


==BolA domain of SufE1 from Arabidopsis thaliana==
<StructureSection load='4pui' size='340' side='right'caption='[[4pui]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pui]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PUI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.698&#8491;</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=4pui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pui OCA], [https://pdbe.org/4pui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pui RCSB], [https://www.ebi.ac.uk/pdbsum/4pui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pui ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SUFE1_ARATH SUFE1_ARATH] Participates in cysteine desulfurization mediated by NFS2 in chloroplast and NIFS1 in mitochondrion (PubMed:16437155). Activates the cysteine desulfurase activity of NFS2 (PubMed:16455656). Cysteine desulfurization mobilizes sulfur from L-cysteine to yield L-alanine and supplies the inorganic sulfur for iron-sulfur (Fe-S) cluster formation. Glutaredoxins regulate SUFE1 activity by inducing its reduction and deglutathionylation (PubMed:24203231).<ref>PMID:16437155</ref> <ref>PMID:16455656</ref> <ref>PMID:24203231</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BolA proteins are defined as stress-responsive transcriptional regulators but they also participate to iron metabolism. Although they can form [2Fe-2S]-containing complexes with monothiol glutaredoxins (Grx), structural details are lacking. Three Arabidopsis thaliana BolA structures were solved. They differ primarily by the size of a loop referred to as the variable [H/C] loop which contains an important cysteine (BolA_C group) or histidine (BolA_H group) residue. From 3D modeling and spectroscopic analyses of A. thaliana GrxS14-BolA1 holo-heterodimer (BolA_H), we provide evidence for the coordination of a Rieske-type [2Fe-2S] cluster. For BolA_C members, the cysteine could replace the histidine as a ligand. NMR interaction experiments using apo-proteins indicate that a completely different heterodimer was formed, involving the nucleic acid binding site of BolA and the C-terminal tail of Grx. The possible biological importance of these complexes is discussed considering the physiological functions previously assigned to BolA and to Grx-BolA or Grx-Grx complexes.

Structural and spectroscopic insights into BolA-glutaredoxin complexes.,Roret T, Tsan P, Couturier J, Zhang B, Johnson MK, Rouhier N, Didierjean C J Biol Chem. 2014 Jul 10. pii: jbc.M114.572701. PMID:25012657<ref>PMID:25012657</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pui" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Didierjean C]]
[[Category: Roret T]]