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PDBsum entry 4uvk
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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 cohesin'S scc3/sa regulatory subunit.
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Authors
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M.B.Roig,
J.Löwe,
K.L.Chan,
F.Beckouët,
J.Metson,
K.Nasmyth.
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Ref.
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Febs Lett, 2014,
588,
3692-3702.
[DOI no: ]
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PubMed id
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Abstract
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Sister chromatid cohesion involves entrapment of sister DNAs by a cohesin ring
created through association of a kleisin subunit (Scc1) with ATPase heads of
Smc1/Smc3 heterodimers. Cohesin's association with chromatin involves subunits
recruited by Scc1: Wapl, Pds5, and Scc3/SA, in addition to Scc2/4 loading
complex. Unlike Pds5, Wapl, and Scc2/4, Scc3s are encoded by all eukaryotic
genomes. Here, a crystal structure of Scc3 reveals a hook-shaped protein
composed of tandem α helices. Its N-terminal domain contains a conserved and
essential surface (CES) present even in organisms lacking Pds5, Wapl, and
Scc2/4, while its C-terminal domain binds a section of the kleisin Scc1. Scc3
turns over in G2/M while maintaining cohesin's association with chromosomes and
it promotes de-acetylation of Smc3 upon Scc1 cleavage.
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