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PDBsum entry 155c
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Electron transport
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PDB id
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155c
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References listed in PDB file
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Key reference
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Title
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The structure of paracoccus denitrificans cytochrome c550.
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Authors
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R.Timkovich,
R.E.Dickerson.
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Ref.
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J Biol Chem, 1976,
251,
4033-4046.
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PubMed id
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Abstract
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The crystal structure of Paracoccus (formerly Micrococcus) denitrificans
cytochrome c550 has been solved by x-ray diffraction to a resolution of 2.45 A.
In both amino acid sequence and molecular structure it is evolutionarily
homologous with mitochondrial cytochrome c from eukaryotes and photosynthetic
cytochrome c2 from purple non-sulfur bacteria. All of these cytochromes c have
the same basic folding pattern, with surface insertions of extra amino acids in
c550. Various strains of c2 have all, some, or none of the extra insertions
observed in c550. The hydrophobic heme environment, position of aromatic rings,
and structure and environment of the heme crevice, are virtually identical in
cytochromes c55o, c, and c2. Radical changes observed at all regions on the
molecular surface except the heme crevice argue for the importance of the
crevice and the exposed edge of the heme in the transfer of electrons to and
from the cytochrome molecule.
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Secondary reference #1
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Title
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Amino acid sequence of paracoccus denitrificans cytochrome c550.
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Authors
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R.Timkovich,
R.E.Dickerson,
E.Margoliash.
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Ref.
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J Biol Chem, 1976,
251,
2197-2206.
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PubMed id
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