View source for 2mma

==NMR-based docking model of GrxS14-BolA2 apo-heterodimer from Arabidopsis thaliana==
<StructureSection load='2mma' size='340' side='right' caption='[[2mma]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mma]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MMA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MMA FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ipz|3ipz]], [[2mm9|2mm9]]</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=2mma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mma OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mma RCSB], [http://www.ebi.ac.uk/pdbsum/2mma PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/GRS14_ARATH GRS14_ARATH]] May only reduce GSH-thiol disulfides, but not protein disulfides (Potential). May protect cells against protein oxidative damage. May regulate CAX cation transporters.<ref>PMID:16829529</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>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Couturier, J]]
[[Category: Didierjean, C]]
[[Category: Roret, T]]
[[Category: Rouhier, N]]
[[Category: Tsan, P]]
[[Category: Gene regulation]]
[[Category: Stress-responsive protein]]
[[Category: Transcriptional regulator]]