PDBsum entry: 1bwe

Electron transport

PDB id: 1bwe

Contents

Protein chain

77 a.a. *

Ligands

SF4 ×2

* Residue conservation analysis

PDB id:

1bwe

Name:

Electron transport

Title:

Artificial fe8s8 ferredoxin: the d13c variant of bacillus schlegelii fe7s8 ferredoxin

Structure:

Protein (ferredoxin). Chain: a. Engineered: yes. Mutation: yes

Source:

Bacillus schlegelii. Organism_taxid: 1484. Atcc: atcc 43741. Collection: atcc 43741. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

S.Aono,D.Bentrop,I.Bertini,G.Cosenza,C.Luchinat

Key ref:

S.Aono et al. (1998). Solution structure of an artificial Fe8S8 ferredoxin: the D13C variant of Bacillus schlegelii Fe7S8 ferredoxin. Eur J Biochem, 258, 502-514. PubMed id: 9874217 DOI: 10.1046/j.1432-1327.1998.2580502.x

Date:

23-Sep-98 Release date: 30-Sep-98

Protein chain

Q45560  (FER_BACSC) -  Ferredoxin 7Fe

Seq: 78 a.a.

Struc: 77 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 

• Biological process: transport (2 terms)
• Biochemical function: electron carrier activity (5 terms)

DOI no: 10.1046/j.1432-1327.1998.2580502.x

Eur J Biochem 258:502-514 (1998)

PubMed id: 9874217

Solution structure of an artificial Fe8S8 ferredoxin: the D13C variant of Bacillus schlegelii Fe7S8 ferredoxin.

S.Aono, D.Bentrop, I.Bertini, G.Cosenza, C.Luchinat.

ABSTRACT

The solution structure of the D13C variant of the thermostable Fe7S8 ferredoxin from Bacillus schlegelii has been determined by 1H-NMR spectroscopy in its oxidized form. In a variable-temperature NMR study the D13C variant was as thermostable (up to 90 degrees C) as the wild-type protein (WT). Seventy-five out of 77 amino acid residues and 81% of all theoretically expected proton resonances in the D13C Fe8S8 protein have been assigned. Its structure was determined through torsion angle dynamics calculations with the program DYANA, using 935 meaningful NOEs (from a total of 1251), hydrogen bond constraints, and NMR-derived dihedral angle constraints for the cluster-ligating cysteines. Afterwards, restrained energy minimization and restrained molecular dynamics were applied to each conformer of the family. The final family of 20 structures has RMSD values from the mean structure of 0.055 nm for the backbone atoms and of 0.099 nm for all heavy atoms. The overall folding of the WT is maintained in the mutant, except for the immediate vicinity of the new cysteine, which becomes much more similar to native Fe8S8 proteins. The two residues at positions 11 and 12, which constitute an insertion with respect to all known Fe8S8 proteins, assume a conformation that does not prevent the preceding and following residues from folding like in native Fe8S8 proteins. Clear evidence for the existence of two conformations involving almost half of the amino acid residues was found. The two conformations are structurally indistinguishable. Temperature-dependent NMR experiments show that one of them is thermodynamically more stable than the other.

Selected figure(s)

Figure 6.
Fig. 6. Pairwise RMSD per residue between the average solution structure of the D13C variant of B. schlegelii Fe7S 8 ferredoxin and of WT (PDB entry 1bd6). Residues 2211 and 16274 were superimposed.

Figure 8.
Fig. 8. Stereo view of the backbone of the average solution structure of D13C highlighting the residues with duplicated resonances (dashed lines). The two clusters and the poorly assigned side chains of residues Tyr2, Ile4, Ile25, Tyr32, and Ile54 (see text) are also shown.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: Eur J Biochem (1998, 258, 502-514) copyright 1998.

Figures were selected by an automated process.