1FER

STRUCTURE AT PH 6.5 OF FERREDOXIN I FROM AZOTOBACTER VINELANDII AT 2.3 ANGSTROMS RESOLUTION

Summary for 1FER

• Entry DOI: 10.2210/pdb1fer/pdb
• Descriptor: FERREDOXIN I, FE3-S4 CLUSTER, IRON/SULFUR CLUSTER, ... (4 entities in total)
• Functional Keywords: electron transfer(iron-sulfur protein)
• Biological source: Azotobacter vinelandii
• Total number of polymer chains: 1
• Total formula weight: 12706.97

Authors

Merritt, E.A.,Stout, G.H.,Turley, S.,Sieker, L.C.,Jensen, L.H.,Orme-Johnson, W.H. (deposition date: 1992-09-02, release date: 1993-04-15, Last modification date: 2024-02-07)

Primary citation

Merritt, E.A.,Stout, G.H.,Turley, S.,Sieker, L.C.,Jehsen, L.H.,Orme-Johnson, W.H.
Structure at pH 6.5 of ferredoxin I from Azotobacter vinelandii at 2.3 A resolution.
Acta Crystallogr.,Sect.D, 49:272-281, 1993

PubMed Abstract: Ferredoxin I from Azotobacter vinelandii (AvFdI) is an iron-sulfur protein composed of 106 amino acids, seven Fe atoms and eight inorganic S* atoms. A crystallographic redetermination of its structure showed the originally reported structure to be incorrect. We report here the crystal structure of AvFdI at pH 6.5. Extensive refinement has led to a final R value of 0.170 for all 6986 non-extinct reflections in the range 10-2.3 A using a solvent model which includes 98 discrete solvent atoms with occupancies between 0.3 and 1.0 and an average B value of 22.5 A(2). The first half of the peptide chain closely resembles that of the 55-residue ferredoxin from Peptococcus aerogenes (PaFd), while the remainder consists of three turns of helix and a series of loops which form a cap over part of the molecular core. Despite the similarities in structure and surroundings, the corresponding 4Fe4S* clusters in PaFd and AvFdI have strikingly different redox potentials; a possible explanation has been sought in the differing hydration models for the two molecules.

PubMed: 15299532
DOI: 10.1107/S0907444992007248

Experimental method

X-RAY DIFFRACTION (2.3 Å)