4PUH

Oxidized BolA2 from Arabidopsis thaliana

Summary for 4PUH

• Entry DOI: 10.2210/pdb4puh/pdb
• Related: 4PUI
• Descriptor: At5g09830 (2 entities in total)
• Functional Keywords: stress-responsive protein, transcriptional regulator, morphogen, protein binding
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Cellular location: Cytoplasm : Q9FIC3
• Total number of polymer chains: 2
• Total formula weight: 20779.68

Authors

Roret, T.,Didierjean, C. (deposition date: 2014-03-13, release date: 2015-04-15, Last modification date: 2024-10-30)

Primary citation

Roret, T.,Tsan, P.,Couturier, J.,Zhang, B.,Johnson, M.K.,Rouhier, N.,Didierjean, C.
Structural and spectroscopic insights into BolA-glutaredoxin complexes.
J.Biol.Chem., 289:24588-24598, 2014

PubMed 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.

PubMed: 25012657
DOI: 10.1074/jbc.M114.572701

Experimental method

X-RAY DIFFRACTION (1.898 Å)