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PDBsum entry 2pcc
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Oxidoreductase/electron transport
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PDB id
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2pcc
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of a complex between electron transfer partners, Cytochrome c peroxidase and cytochrome c.
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Authors
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H.Pelletier,
J.Kraut.
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Ref.
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Science, 1992,
258,
1748-1755.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of a 1:1 complex between yeast cytochrome c peroxidase and
yeast iso-1-cytochrome c was determined at 2.3 A resolution. This structure
reveals a possible electron transfer pathway unlike any previously proposed for
this extensively studied redox pair. The shortest straight line between the two
hemes closely follows the peroxidase backbone chain of residues Ala194, Ala193,
Gly192, and finally Trp191, the indole ring of which is perpendicular to, and in
van der Waals contact with, the peroxidase heme. The crystal structure at 2.8 A
of a complex between yeast cytochrome c peroxidase and horse heart cytochrome c
was also determined. Although crystals of the two complexes (one with cytochrome
c from yeast and the other with cytochrome c from horse) grew under very
different conditions and belong to different space groups, the two complex
structures are closely similar, suggesting that cytochrome c interacts with its
redox partners in a highly specific manner.
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Secondary reference #1
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Title
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X-Ray structures of recombinant yeast cytochrome c peroxidase and three heme-Cleft mutants prepared by site-Directed mutagenesis.
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Authors
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J.M.Wang,
M.Mauro,
S.L.Edwards,
S.J.Oatley,
L.A.Fishel,
V.A.Ashford,
N.H.Xuong,
J.Kraut.
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Ref.
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Biochemistry, 1990,
29,
7160-7173.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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High-Resolution refinement of yeast iso-1-Cytochrome c and comparisons with other eukaryotic cytochromes c.
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Authors
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G.V.Louie,
G.D.Brayer.
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Ref.
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J Mol Biol, 1990,
214,
527-555.
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PubMed id
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