4pug: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
</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=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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.998Å</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=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> | |||
</table> | </table> | ||
== Function == | == Function == | ||
Latest revision as of 20:22, 20 September 2023
BolA1 from Arabidopsis thalianaBolA1 from Arabidopsis thaliana
Structural highlights
FunctionBOLA1_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).[1] [2] 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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