1BD6

7-FE FERREDOXIN FROM BACILLUS SCHLEGELII, NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 1BD6

• Entry DOI: 10.2210/pdb1bd6/pdb
• NMR Information: BMRB: 4268
• Descriptor: 7-FE FERREDOXIN, FE3-S4 CLUSTER, IRON/SULFUR CLUSTER (3 entities in total)
• Functional Keywords: electron transport, iron-sulfur
• Biological source: Bacillus schlegelii
• Total number of polymer chains: 1
• Total formula weight: 9398.26

Authors

Aono, S.,Bentrop, D.,Bertini, I.,Donaire, A.,Luchinat, C.,Niikura, Y.,Rosato, A. (deposition date: 1998-05-06, release date: 1998-06-17, Last modification date: 2024-05-22)

Primary citation

Aono, S.,Bentrop, D.,Bertini, I.,Donaire, A.,Luchinat, C.,Niikura, Y.,Rosato, A.
Solution structure of the oxidized Fe7S8 ferredoxin from the thermophilic bacterium Bacillus schlegelii by 1H NMR spectroscopy.
Biochemistry, 37:9812-9826, 1998

PubMed Abstract: The solution structure of the paramagnetic seven-iron ferredoxin from Bacillus schlegelii in its oxidized form has been determined by 1H NMR. The protein, which contains 77 amino acids, is thermostable. Seventy-two residues and 79% of all theoretically expected proton resonances have been assigned. The structure has been determined through torsion angle dynamics calculations with the program DYANA, using 966 meaningful NOEs (from a total of 1305), hydrogen bond constraints, and NMR derived dihedral angle constraints for the cluster ligating cysteines, and by using crystallographic information to build up the two clusters. 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 0.68 A for the backbone atoms and of 1.16 A for all heavy atoms. The contributions to the thermal stability of the B. schlegelii ferredoxin are discussed by comparing the present structure to that of the less stable Azotobacter vinelandii ferredoxin I which is the only other available structure of a bacterial seven-iron ferredoxin. It is proposed that the hydrophobic interactions and the hydrogen bond network linking the N-terminus and the C-terminus together and a high number of salt bridges contribute to the stability.

PubMed: 9657695
DOI: 10.1021/bi972818b

Experimental method

SOLUTION NMR