Crystal structure of the 16 heme cytochrome from Desulfovibrio gigas: a glycosylated protein in a sulphate-reducing bacterium. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Molecular Biology Année : 2007

Crystal structure of the 16 heme cytochrome from Desulfovibrio gigas: a glycosylated protein in a sulphate-reducing bacterium.

Teresa Santos-Silva
  • Fonction : Auteur
João Miguel Dias
  • Fonction : Auteur
Alain Dolla
Luísa L Gonçalves
  • Fonction : Auteur
Jorge Lampreia
  • Fonction : Auteur
Maria João Romão
  • Fonction : Auteur

Résumé

Sulphate-reducing bacteria have a wide variety of periplasmic cytochromes involved in electron transfer from the periplasm to the cytoplasm. HmcA is a high molecular mass cytochrome of 550 amino acid residues that harbours 16 c-type heme groups. We report the crystal structure of HmcA isolated from the periplasm of Desulfovibrio gigas. Crystals were grown using polyethylene glycol 8K and zinc acetate, and diffracted beyond 2.1 A resolution. A multiple-wavelength anomalous dispersion experiment at the iron absorption edge enabled us to obtain good-quality phases for structure solution and model building. DgHmcA has a V-shape architecture, already observed in HmcA isolated from Desulfovibrio vulgaris Hildenborough. The presence of an oligosaccharide molecule covalently bound to an Asn residue was observed in the electron density maps of DgHmcA and confirmed by mass spectrometry. Three modified monosaccharides appear at the highly hydrophobic vertex, possibly acting as an anchor of the protein to the cytoplasmic membrane.

Dates et versions

hal-00475650 , version 1 (22-04-2010)

Identifiants

Citer

Teresa Santos-Silva, João Miguel Dias, Alain Dolla, Marie-Claire Durand, Luísa L Gonçalves, et al.. Crystal structure of the 16 heme cytochrome from Desulfovibrio gigas: a glycosylated protein in a sulphate-reducing bacterium.. Journal of Molecular Biology, 2007, 370 (4), pp.659-73. ⟨10.1016/j.jmb.2007.04.055⟩. ⟨hal-00475650⟩

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