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| | ==BolA domain of SufE1 from Arabidopsis thaliana== | | ==BolA domain of SufE1 from Arabidopsis thaliana== |
| - | <StructureSection load='4pui' size='340' side='right' caption='[[4pui]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='4pui' size='340' side='right'caption='[[4pui]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pui]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PUI FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4puh|4puh]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.698Å</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=4pui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pui OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pui RCSB], [http://www.ebi.ac.uk/pdbsum/4pui PDBsum]</span></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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SUFE_ARATH SUFE_ARATH]] Participates in cysteine desulfurization mediated by NFS2 in chloroplast and NIFS1 in mitochondrion. Can activate the cysteine desulfurase activity of NFS2. Cysteine desulfurization mobilizes sulfur from L-cysteine to yield L-alanine and supplies the inorganic sulfur for iron-sulfur (Fe-S) cluster formation.<ref>PMID:16437155</ref> <ref>PMID:16455656</ref> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4pui" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Didierjean, C]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Roret, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Metal binding protein]] | + | [[Category: Didierjean C]] |
| - | [[Category: Protein binding]] | + | [[Category: Roret T]] |
| - | [[Category: Protein binding protein]]
| + | |
| - | [[Category: Stress-responsive protein]]
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| Structural highlights
Function
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).[1] [2] [3]
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu XM, Moller SG. AtSufE is an essential activator of plastidic and mitochondrial desulfurases in Arabidopsis. EMBO J. 2006 Feb 22;25(4):900-9. Epub 2006 Jan 26. PMID:16437155 doi:http://dx.doi.org/10.1038/sj.emboj.7600968
- ↑ Ye H, Abdel-Ghany SE, Anderson TD, Pilon-Smits EA, Pilon M. CpSufE activates the cysteine desulfurase CpNifS for chloroplastic Fe-S cluster formation. J Biol Chem. 2006 Mar 31;281(13):8958-69. Epub 2006 Feb 2. PMID:16455656 doi:http://dx.doi.org/10.1074/jbc.M512737200
- ↑ Couturier J, Wu HC, Dhalleine T, Pégeot H, Sudre D, Gualberto JM, Jacquot JP, Gaymard F, Vignols F, Rouhier N. Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis thaliana BolA2 and SufE1. Mol Plant. 2014 Jan;7(1):187-205. PMID:24203231 doi:10.1093/mp/sst156
- ↑ Roret T, Tsan P, Couturier J, Zhang B, Johnson MK, Rouhier N, Didierjean C. Structural and spectroscopic insights into BolA-glutaredoxin complexes. J Biol Chem. 2014 Jul 10. pii: jbc.M114.572701. PMID:25012657 doi:http://dx.doi.org/10.1074/jbc.M114.572701
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