2mma: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[2mma]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2MMA FirstGlance]. <br>
-</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=2mma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mma OCA], [https://pdbe.org/2mma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mma RCSB], [https://www.ebi.ac.uk/pdbsum/2mma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mma ProSAT]</span></td></tr>
+</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=2mma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mma OCA], [https://pdbe.org/2mma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mma RCSB], [https://www.ebi.ac.uk/pdbsum/2mma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mma ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://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>
-<div class="pdbe-citations 2mma" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>