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PDBsum entry 6f4m
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Oxidoreductase
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PDB id
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6f4m
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References listed in PDB file
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Key reference
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Title
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Jmjd5 is a human arginyl c-3 hydroxylase.
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Authors
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S.E.Wilkins,
S.Islam,
J.M.Gannon,
S.Markolovic,
R.J.Hopkinson,
W.Ge,
C.J.Schofield,
R.Chowdhury.
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Ref.
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Nat Commun, 2018,
9,
1180.
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PubMed id
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Abstract
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Oxygenase-catalysed post-translational modifications of basic protein residues,
including lysyl hydroxylations and Nε-methyl lysyl demethylations,
have important cellular roles. Jumonji-C (JmjC) domain-containing protein 5
(JMJD5), which genetic studies reveal is essential in animal development, is
reported as a histone Nε-methyl lysine demethylase (KDM). Here we
report how extensive screening with peptides based on JMJD5 interacting proteins
led to the finding that JMJD5 catalyses stereoselective C-3 hydroxylation of
arginine residues in sequences from human regulator of chromosome condensation
domain-containing protein 1 (RCCD1) and ribosomal protein S6 (RPS6).
High-resolution crystallographic analyses reveal overall fold, active site and
substrate binding/product release features supporting the assignment of JMJD5 as
an arginine hydroxylase rather than a KDM. The results will be useful in the
development of selective oxygenase inhibitors for the treatment of cancer and
genetic diseases.
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