4puh: Difference between revisions

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'''Unreleased structure'''


The entry 4puh is ON HOLD
==Oxidized BolA2 from Arabidopsis thaliana==
<StructureSection load='4puh' size='340' side='right'caption='[[4puh]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4puh]] 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=4PUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PUH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.898&#8491;</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=4puh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4puh OCA], [https://pdbe.org/4puh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4puh RCSB], [https://www.ebi.ac.uk/pdbsum/4puh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4puh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BOLA2_ARATH BOLA2_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 GRXS17-BOLA2 heterodimer binds a labile, oxygen sensitive iron-sulfur cluster (PubMed:24714563).<ref>PMID:24714563</ref> <ref>PMID:24203231</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.


Authors: Roret, T., Didierjean, C.
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>


Description: Oxidized BolA2 from Arabidopsis thaliana
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4puh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Didierjean C]]
[[Category: Roret T]]
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