2mma: Difference between revisions
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<StructureSection load='2mma' size='340' side='right' caption='[[2mma]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='2mma' size='340' side='right' caption='[[2mma]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == 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> | <table><tr><td colspan='2'>[[2mma]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. 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> | </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://pdbe.org/2mma PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mma RCSB], [http://www.ebi.ac.uk/pdbsum/2mma PDBsum]</span></td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRXS14, CXIP1, At3g54900, F28P10.120 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), AT5G09830, At5g09830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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://pdbe.org/2mma PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mma RCSB], [http://www.ebi.ac.uk/pdbsum/2mma PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mma ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arath]] | |||
[[Category: Couturier, J]] | [[Category: Couturier, J]] | ||
[[Category: Didierjean, C]] | [[Category: Didierjean, C]] | ||
Revision as of 01:53, 10 August 2018
NMR-based docking model of GrxS14-BolA2 apo-heterodimer from Arabidopsis thalianaNMR-based docking model of GrxS14-BolA2 apo-heterodimer from Arabidopsis thaliana
Structural highlights
Function[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.[1] Publication Abstract from PubMedBolA 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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