PDBsum entry 4pui

Protein binding

PDB id: 4pui

Contents

Protein chains

85 a.a.

86 a.a.

Waters ×165

PDB id:

4pui

Name:

Protein binding

Title:

Bola domain of sufe1 from arabidopsis thaliana

Structure:

Sufe-like protein, chloroplastic. Chain: a, b. Fragment: unp residues 277-371. Synonym: protein embryo defective 1374, protein sulfur e, atsufe, protein sulfur e 1, atsufe1. Engineered: yes

Source:

Arabidopsis thaliana. Mouse-ear cress,thale-cress. Organism_taxid: 3702. Gene: sufe, emb1374, sufe1, at4g26500, m3e9.70. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.70Å R-factor: 0.192 R-free: 0.213

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

Q84W65  (SUFE1_ARATH) -  SufE-like protein 1, chloroplastic/mitochondrial from Arabidopsis thaliana

Seq: 371 a.a.

Struc: 85 a.a.

Protein chain

Q84W65  (SUFE1_ARATH) -  SufE-like protein 1, chloroplastic/mitochondrial from Arabidopsis thaliana

Seq: 371 a.a.

Struc: 86 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.