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

Autor: Jorge Lampreia, Maria João Romão, Luísa L. Gonçalves, Teresa Santos-Silva, Marie-Claire Durand, Alain Dolla, Isabel Moura, João M. Dias
Přispěvatelé: Interactions et Modulateurs de Réponses (IMR), Centre National de la Recherche Scientifique (CNRS), Departamento de Quimica (REQUIMTE), Universidade de Lisboa (ULISBOA)-Centro de Quimica Fina e Biotecnologia
Jazyk: angličtina
Rok vydání: 2007
Předmět:
Models
Molecular
Glycosylation
Cytochrome
MESH: Protein Structure
Secondary
MESH: Amino Acid Sequence
Crystallography
X-Ray
Protein Structure
Secondary
chemistry.chemical_compound
MESH: Protein Structure
Tertiary
Structural Biology
Desulfovibrio gigas
Desulfovibrio vulgaris
Heme
MESH: Cytochromes
Conserved Sequence
MESH: Static Electricity
MESH: Structural Homology
Protein
0303 health sciences
MESH: Conserved Sequence
biology
Chemistry
MESH: Glycosylation
Biochemistry
MESH: Heme
MESH: Models
Molecular
Stereochemistry
Molecular Sequence Data
Static Electricity
MESH: Sequence Alignment
MESH: Desulfovibrio gigas
03 medical and health sciences
Electron transfer
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Amino Acid Sequence
Molecular Biology
030304 developmental biology
MESH: Molecular Sequence Data
Molecular mass
030306 microbiology
Periplasmic space
biology.organism_classification
MESH: Crystallography
X-Ray
Protein Structure
Tertiary
Heme C
Structural Homology
Protein
biology.protein
Cytochromes
Sequence Alignment
Zdroj: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2007, 370 (4), pp.659-73. ⟨10.1016/j.jmb.2007.04.055⟩
ISSN: 0022-2836
1089-8638
DOI: 10.1016/j.jmb.2007.04.055⟩
Popis: International audience; 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.
Databáze: OpenAIRE
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