PDBsum entry 4pui

Protein binding

PDB id: 4pui

Contents

Protein chains

85 a.a.

86 a.a.

Waters ×165

References listed in PDB file

Key reference

• Title: Structural and spectroscopic insights into bola-Glutaredoxin complexes.
• Authors: T.Roret, P.Tsan, J.Couturier, B.Zhang, M.K.Johnson, N.Rouhier, C.Didierjean.
• Ref.: J Biol Chem, 2014, 289, 24588-24598. [DOI no: 10.1074/jbc.M114.572701]
• PubMed id: 25012657

Abstract

BolA proteins are defined as stress-responsive transcriptional regulators, but they also participate in 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 three-dimensional 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 apoproteins 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.