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PDBsum entry 6f6c
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Oxidoreductase
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PDB id
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6f6c
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References listed in PDB file
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Key reference
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Title
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Ether cross-Link formation in the r2-Like ligand-Binding oxidase.
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Authors
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J.J.Griese,
R.M.M.Branca,
V.Srinivas,
M.Högbom.
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Ref.
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J Biol Inorg Chem, 2018,
23,
879-886.
[DOI no: ]
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PubMed id
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Abstract
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R2-like ligand-binding oxidases contain a dinuclear metal cofactor which can
consist either of two iron ions or one manganese and one iron ion, but the
heterodinuclear Mn/Fe cofactor is the preferred assembly in the presence of
MnII and FeII in vitro. We have previously shown that both
types of cofactor are capable of catalyzing formation of a tyrosine-valine ether
cross-link in the protein scaffold. Here we demonstrate that Mn/Fe centers
catalyze cross-link formation more efficiently than Fe/Fe centers, indicating
that the heterodinuclear cofactor is the biologically relevant one. We further
explore the chemical potential of the Mn/Fe cofactor by introducing mutations at
the cross-linking valine residue. We find that cross-link formation is possible
also to the tertiary beta-carbon in an isoleucine, but not to the secondary
beta-carbon or tertiary gamma-carbon in a leucine, nor to the primary
beta-carbon of an alanine. These results illustrate that the reactivity of the
cofactor is highly specific and directed.
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