PDBsum entry 1dox

Electron transport

PDB id: 1dox

Contents

Protein chain

96 a.a.

Ligands

FES

References listed in PDB file

Key reference

• Title: 1h and 15n nmr sequential assignment, Secondary structure, And tertiary fold of [2fe-2s] ferredoxin from synechocystis sp. Pcc 6803.
• Authors: C.Lelong, P.Sétif, H.Bottin, F.André, J.M.Neumann.
• Ref.: Biochemistry, 1995, 34, 14462-14473.
• PubMed id: 7578051

Abstract

The [2Fe-2S] ferredoxin extracted from Synechocystis sp. PCC 6803 was studied by 1H and 15N nuclear magnetic resonance. Sequence-specific 1H and 15N assignment of amino acid residues far from the paramagnetic cluster (distance higher than 8 A) was performed. Interresidue NOE constraints have allowed the identification of several secondary structure elements: one beta sheet composed of four beta strands, one alpha helix, and two alpha helix turns. The analysis of interresidue NOEs suggests the existence of a disulfide bridge between the cysteine residues 18 and 85. Such a disulfide bridge has never been observed in plant-type ferredoxins. Structure modeling using the X-PLOR program was performed with or without assuming the existence of a disulfide bridge. As a result, two structure families were obtained with rms deviations of 2.2 A. Due to the lack of NOE connectivities resulting from the paramagnetic effect from the [2Fe-2S] cluster, the structures were not well resolved in the region surrounding the [2Fe-2S] cluster, at both extremities of the alpha helix and the C and N terminus segments. In contrast, when taken separately, the beta sheet and the alpha helix were well defined. This work is the first report of a structure model of a plant-type [2Fe-2S] Fd in solution.

Secondary reference #1

• Title: Ferredoxin and flavodoxin from the cyanobacterium synechocystis sp pcc 6803.
• Authors: H.Bottin, B.Lagoutte.
• Ref.: Biochim Biophys Acta, 1992, 1101, 48-56.
• PubMed id: 1633177