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2mma
From Proteopedia
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| - | ''' | + | ==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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ipz|3ipz]], [[2mm9|2mm9]]</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=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> | ||
| + | <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®/PubMed®, 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]] | ||
Revision as of 07:50, 23 July 2014
NMR-based docking model of GrxS14-BolA2 apo-heterodimer from Arabidopsis thaliana
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