4pug

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'''Unreleased structure'''
 
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The entry 4pug is ON HOLD until Paper Publication
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==BolA1 from Arabidopsis thaliana==
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<StructureSection load='4pug' size='340' side='right'caption='[[4pug]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4pug]] 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=4PUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PUG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.998&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pug OCA], [https://pdbe.org/4pug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pug RCSB], [https://www.ebi.ac.uk/pdbsum/4pug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pug ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BOLA1_ARATH BOLA1_ARATH] May act either alone or in interaction with glutaredoxin as a redox-regulated transcriptional regulator, or as a factor regulating Fe-S cluster biogenesis (Probable). The glutaredoxin-BOLA1 heterodimers bind a labile, oxygen sensitive iron-sulfur cluster (PubMed:24714563).<ref>PMID:24714563</ref> <ref>PMID:24203231</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Roret, T., Didierjean, C.
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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>
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Description: BolA1 from Arabidopsis thaliana
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4pug" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Arabidopsis thaliana]]
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[[Category: Large Structures]]
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[[Category: Didierjean C]]
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[[Category: Roret T]]

Current revision

BolA1 from Arabidopsis thaliana

PDB ID 4pug

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