ORIGINAL ARTICLE

JBIC Journal of Biological Inorganic Chemistry

, Volume 2, Issue 6, pp 680-689

First online:

Desulfoferrodoxin structure determined by MAD phasing and refinement to 1.9-Å resolution reveals a unique combination of a tetrahedral FeS4 centre with a square pyramidal FeSN4 centre

  • Ana V. CoelhoAffiliated withChemistry Department, Universidade de Évora, P-7000 Évora, Portugal
  • , Pedro MatiasAffiliated withInstituto de Tecnologia Química e Biológica, Apartado 127, P-2780 Oeiras, Portugal
  • , Vilmos FülöpAffiliated withLaboratory of Molecular Biophysics and Oxford Centre for Molecular Sciences, University of Oxford, South Parks Road, Oxford OX1 3QU, UK
  • , Andrew ThompsonAffiliated withEMBL Grenoble Outstation, c/o ILL 20, BP-156, F-38042 Grenoble Cedex, France
  • , A. GonzalezAffiliated withESRF, BP-220, F-38043 Grenoble Cedex, France
  • , M. A. CarrondoAffiliated withInstituto de Tecnologia Química e Biológica, Apartado 127, P-2780 Oeiras, Portugal

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Abstract

 The structure of desulfoferrodoxin (DFX), a protein containing two mononuclear non-heme iron centres, has been solved by the MAD method using phases determined at 2.8 Å resolution. The iron atoms in the native protein were used as the anomalous scatterers. The model was built from an electron density map obtained after density modification and refined against data collected at 1.9 Å. Desulfoferrodoxin is a homodimer which can be described in terms of two domains, each with two crystallographically equivalent non-heme mononuclear iron centres. Domain I is similar to desulforedoxin with distorted rubredoxin-type centres, and domain II has iron centres with square pyramidal coordination to four nitrogens from histidines as the equatorial ligands and one sulfur from a cysteine as the axial ligand. Domain I in DFX shows a remarkable structural fit with the DX homodimer. Furthermore, three β-sheets extending from one monomer to another in DFX, two in domain I and one in domain II, strongly support the assumption of DFX as a functional dimer. A calcium ion, indispensable in the crystallisation process, was assumed at the dimer interface and appears to contribute to dimer stabilisation. The C-terminal domain in the monomer has a topology fold similar to that of fibronectin III.

Key words Desulfoferrodoxin Non-heme iron centre MAD method Rubredoxin Fibronectin III