4pui | pdb_00004pui
BolA domain of SufE1 from Arabidopsis thaliana
Structural highlights
FunctionSUFE1_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 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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