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PDBsum entry 1ryc
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Oxidoreductase
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PDB id
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1ryc
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References listed in PDB file
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Key reference
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Title
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A ligand-Gated, Hinged loop rearrangement opens a channel to a buried artificial protein cavity.
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Authors
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M.M.Fitzgerald,
R.A.Musah,
D.E.Mcree,
D.B.Goodin.
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Ref.
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Nat Struct Biol, 1996,
3,
626-631.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
90%.
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Abstract
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Conformational changes that gate the access of substrates or ligands to an
active site are important features of enzyme function. In this report, we
describe an unusual example of a structural rearrangement near a buried
artificial cavity in cytochrome c peroxidase that occurs on binding protonated
benzimidazole. A hinged main-chain rotation at two residues (Pro 190 and Asn
195) results in a surface loop rearrangement that opens a large
solvent-accessible channel for the entry of ligands to an otherwise inaccessible
binding site. The trapping of this alternate conformational state provides a
unique view of the extent to which protein dynamics can allow small molecule
penetration into buried protein cavities.
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Secondary reference #1
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Title
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The role of aspartate-235 in the binding of cations to an artificial cavity at the radical site of cytochrome c peroxidase.
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Authors
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M.M.Fitzgerald,
M.L.Trester,
G.M.Jensen,
D.E.Mcree,
D.B.Goodin.
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Ref.
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Protein Sci, 1995,
4,
1844-1850.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Small molecule binding to an artificially created cavity at the active site of cytochrome c peroxidase.
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Authors
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M.M.Fitzgerald,
M.J.Churchill,
D.E.Mcree,
D.B.Goodin.
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Ref.
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Biochemistry, 1994,
33,
3807-3818.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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The asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, Electronic structure, And coupling of the tryptophan free radical to the heme.
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Authors
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D.B.Goodin,
D.E.Mcree.
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Ref.
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Biochemistry, 1993,
32,
3313-3324.
[DOI no: ]
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PubMed id
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