PDBsum entry 4pug

DNA binding protein

PDB id: 4pug

Contents

Protein chains

94 a.a.

84 a.a.

Waters ×206

PDB id:

4pug

Name:

DNA binding protein

Title:

Bola1 from arabidopsis thaliana

Structure:

Bola like protein. Chain: a, b. Fragment: unp residues 64-160. Synonym: bola-like protein. Engineered: yes

Source:

Arabidopsis thaliana. Mouse-ear cress,thale-cress. Organism_taxid: 3702. Gene: at1g55805, at1g55805. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.00Å R-factor: 0.201 R-free: 0.226

Authors:

T.Roret,C.Didierjean

Key ref:

T.Roret et al. (2014). Structural and spectroscopic insights into BolA-glutaredoxin complexes. J Biol Chem, 289, 24588-24598. PubMed id: 25012657 DOI: 10.1074/jbc.M114.572701

Date:

13-Mar-14 Release date: 23-Jul-14

Protein chain

Q682I1  (BOLA1_ARATH) -  Protein BOLA1, chloroplastic from Arabidopsis thaliana

Seq: 160 a.a.

Struc: 94 a.a.

Protein chain

Q682I1  (BOLA1_ARATH) -  Protein BOLA1, chloroplastic from Arabidopsis thaliana

Seq: 160 a.a.

Struc: 84 a.a.

DOI no: 10.1074/jbc.M114.572701

J Biol Chem 289:24588-24598 (2014)

PubMed id: 25012657

Structural and spectroscopic insights into BolA-glutaredoxin complexes.

T.Roret, P.Tsan, J.Couturier, B.Zhang, M.K.Johnson, N.Rouhier, C.Didierjean.

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.