2MM9

Solution structure of reduced BolA2 from Arabidopsis thaliana

Summary for 2MM9

• Entry DOI: 10.2210/pdb2mm9/pdb
• NMR Information: BMRB: 19849
• Descriptor: BolA2 (1 entity in total)
• Functional Keywords: stress-responsive protein, transcriptional regulator, morphogen, transcription
• Biological source: Arabidopsis thaliana (mouse-ear cress)
• Total number of polymer chains: 1
• Total formula weight: 10389.84

Authors

Roret, T.,Tsan, P.,Couturier, J.,Rouhier, N.,Didierjean, C. (deposition date: 2014-03-13, release date: 2014-07-23, Last modification date: 2024-05-01)

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

SOLUTION NMR