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PDBsum entry 5e3b
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References listed in PDB file
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Key reference
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Title
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Disruption of macrodomain protein sco6735 increases antibiotic production in streptomyces coelicolor.
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Authors
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J.Lalić,
M.Posavec marjanović,
L.Palazzo,
D.Perina,
I.Sabljić,
R.ŽAja,
T.Colby,
B.Pleše,
M.Halasz,
G.Jankevicius,
G.Bucca,
M.Ahel,
I.Matić,
H.ĆEtković,
M.Luić,
A.Mikoč,
I.Ahel.
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Ref.
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J Biol Chem, 2016,
291,
23175-23187.
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PubMed id
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Abstract
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ADP-ribosylation is a post-translational modification that can alter the
physical and chemical properties of target proteins and that controls many
important cellular processes. Macrodomains are evolutionarily conserved
structural domains that bind ADP-ribose derivatives and are found in proteins
with diverse cellular functions. Some proteins from the macrodomain family can
hydrolyze ADP-ribosylated substrates and therefore reverse this
post-translational modification. Bacteria and Streptomyces, in particular, are
known to utilize protein ADP-ribosylation, yet very little is known about their
enzymes that synthesize and remove this modification. We have determined the
crystal structure and characterized, both biochemically and functionally, the
macrodomain protein SCO6735 from Streptomyces coelicolor This protein is a
member of an uncharacterized subfamily of macrodomain proteins. Its crystal
structure revealed a highly conserved macrodomain fold. We showed that SCO6735
possesses the ability to hydrolyze PARP-dependent protein ADP-ribosylation.
Furthermore, we showed that expression of this protein is induced upon DNA
damage and that deletion of this protein in S. coelicolor increases antibiotic
production. Our results provide the first insights into the molecular basis of
its action and impact on Streptomyces metabolism.
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