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PDBsum entry 2vld
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References listed in PDB file
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Key reference
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Title
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Structure and function of a novel endonuclease acting on branched DNA substrates.
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Authors
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B.Ren,
J.Kühn,
L.Meslet-Cladiere,
J.Briffotaux,
C.Norais,
R.Lavigne,
D.Flament,
R.Ladenstein,
H.Myllykallio.
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Ref.
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Embo J, 2009,
28,
2479-2489.
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PubMed id
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Abstract
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We show that Pyrococcus abyssi PAB2263 (dubbed NucS (nuclease for ss DNA) is a
novel archaeal endonuclease that interacts with the replication clamp PCNA.
Structural determination of P. abyssi NucS revealed a two-domain dumbbell-like
structure that in overall does not resemble any known protein structure.
Biochemical and structural studies indicate that NucS orthologues use a
non-catalytic ssDNA-binding domain to regulate the cleavage activity at another
site, thus resulting into the specific cleavage at double-stranded DNA
(dsDNA)/ssDNA junctions on branched DNA substrates. Both 3' and 5' extremities
of the ssDNA can be cleaved at the nuclease channel that is too narrow to
accommodate duplex DNA. Altogether, our data suggest that NucS proteins
constitute a new family of structure-specific DNA endonucleases that are widely
distributed in archaea and in bacteria, including Mycobacterium tuberculosis.
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