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PDBsum entry 4i99
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DNA binding protein
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PDB id
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4i99
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References listed in PDB file
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Key reference
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Title
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An asymmetric smc-Kleisin bridge in prokaryotic condensin.
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Authors
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F.Bürmann,
H.C.Shin,
J.Basquin,
Y.M.Soh,
V.Giménez-Oya,
Y.G.Kim,
B.H.Oh,
S.Gruber.
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Ref.
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Nat Struct Biol, 2013,
20,
371-379.
[DOI no: ]
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PubMed id
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Abstract
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Eukaryotic structural maintenance of chromosomes (SMC)-kleisin complexes form
large, ring-shaped assemblies that promote accurate chromosome segregation.
Their asymmetric structural core comprises SMC heterodimers that associate with
both ends of a kleisin subunit. However, prokaryotic condensin Smc-ScpAB is
composed of symmetric Smc homodimers associated with the kleisin ScpA in a
postulated symmetrical manner. Here, we demonstrate that Smc molecules have two
distinct binding sites for ScpA. The N terminus of ScpA binds the Smc coiled
coil, whereas the C terminus binds the Smc ATPase domain. We show that in
Bacillus subtilis cells, an Smc dimer is bridged by a single ScpAB to generate
asymmetric tripartite rings analogous to eukaryotic SMC complexes. We define a
molecular mechanism that ensures asymmetric assembly, and we conclude that the
basic architecture of SMC-kleisin rings evolved before the emergence of
eukaryotes.
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