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PDBsum entry 5eyb
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DNA binding protein/DNA
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PDB id
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5eyb
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PDB id:
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| Name: |
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DNA binding protein/DNA
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Title:
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X-ray structure of reb1-ter complex
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Structure:
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DNA-binding protein reb1. Chain: a, b. Fragment: unp residues 146-504. Engineered: yes. DNA (26-mer). Chain: c, e. Engineered: yes. DNA (26-mer). Chain: d, f.
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Source:
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Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 284812. Strain: 972 / atcc 24843. Gene: reb1, spbc1198.11c, spbc660.01c. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Synthetic construct.
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Resolution:
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2.70Å
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R-factor:
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0.212
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R-free:
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0.243
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Authors:
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R.Jaiswal,M.Choudhury,S.Zaman,S.Singh,V.Santosh,D.Bastia, C.R.Escalante
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Key ref:
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R.Jaiswal
et al.
(2016).
Functional architecture of the Reb1-Ter complex of Schizosaccharomyces pombe.
Proc Natl Acad Sci U S A,
113,
E2267.
PubMed id:
DOI:
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Date:
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24-Nov-15
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Release date:
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13-Apr-16
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PROCHECK
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Headers
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References
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Q9P6H9
(REB1_SCHPO) -
DNA-binding protein reb1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843)
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Seq:
Struc:
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504 a.a.
340 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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G-T-A-A-A-A-G-G-T-A-A-G-G-G-T-A-A-T-G-C-A-C-T-T-T-T
26 bases
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C-A-A-A-A-G-T-G-C-A-T-T-A-C-C-C-T-T-A-C-C-T-T-T-T-A
26 bases
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G-T-A-A-A-A-G-G-T-A-A-G-G-G-T-A-A-T-G-C-A-C-T-T-T-T
26 bases
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C-A-A-A-A-G-T-G-C-A-T-T-A-C-C-C-T-T-A-C-C-T-T-T-T-A
26 bases
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DOI no:
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Proc Natl Acad Sci U S A
113:E2267
(2016)
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PubMed id:
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Functional architecture of the Reb1-Ter complex of Schizosaccharomyces pombe.
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R.Jaiswal,
M.Choudhury,
S.Zaman,
S.Singh,
V.Santosh,
D.Bastia,
C.R.Escalante.
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ABSTRACT
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Reb1 ofSchizosaccharomyces pomberepresents a family of multifunctional proteins
that bind to specific terminator sites (Ter) and cause polar termination of
transcription catalyzed by RNA polymerase I (pol I) and arrest of replication
forks approaching the Ter sites from the opposite direction. However, it remains
to be investigated whether the same mechanism causes arrest of both DNA
transactions. Here, we present the structure of Reb1 as a complex with a Ter
site at a resolution of 2.7 Å. Structure-guided molecular genetic analyses
revealed that it has distinct and well-defined DNA binding and transcription
termination (TTD) domains. The region of the protein involved in replication
termination is distinct from the TTD. Mechanistically, the data support the
conclusion that transcription termination is not caused by just high affinity
Reb1-Ter protein-DNA interactions. Rather, protein-protein interactions between
the TTD with the Rpa12 subunit of RNA pol I seem to be an integral part of the
mechanism. This conclusion is further supported by the observation that double
mutations in TTD that abolished its interaction with Rpa12 also greatly reduced
transcription termination thereby revealing a conduit for functional
communications between RNA pol I and the terminator protein.
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Links
