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PDBsum entry 4ejs
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Transcription
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PDB id
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4ejs
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Contents |
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223 a.a.
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221 a.a.
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271 a.a.
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PDB id:
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Transcription
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Title:
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Structure of yeast elongator subcomplex elp456
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Structure:
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Elongator complex protein 4. Chain: a. Fragment: unp residues 67-438. Synonym: gamma-toxin target 7, hat-associated protein 1. Engineered: yes. Elongator complex protein 5. Chain: b. Fragment: unp residues 1-238. Synonym: gamma-toxin target 5, hat-associated protein 2, protein
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Source:
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Saccharomyces cerevisiae. Yeast. Organism_taxid: 559292. Strain: s288c. Gene: elp4. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: elp5. Gene: elp6.
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Resolution:
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2.61Å
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R-factor:
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0.176
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R-free:
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0.224
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Authors:
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Z.Lin,W.Zhao,J.Long,Y.Shen
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Key ref:
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Z.Lin
et al.
(2012).
Crystal structure of elongator subcomplex Elp4-6.
J Biol Chem,
287,
21501-21508.
PubMed id:
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Date:
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07-Apr-12
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Release date:
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02-May-12
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PROCHECK
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Headers
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References
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Q02884
(ELP4_YEAST) -
Elongator complex protein 4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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456 a.a.
223 a.a.
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J Biol Chem
287:21501-21508
(2012)
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PubMed id:
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Crystal structure of elongator subcomplex Elp4-6.
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Z.Lin,
W.Zhao,
W.Diao,
X.Xie,
Z.Wang,
J.Zhang,
Y.Shen,
J.Long.
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ABSTRACT
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Elongator is a multiprotein complex composed of two subcomplexes, Elp1-3 and
Elp4-6. Elongator is highly conserved between yeast and humans and plays an
important role in RNA polymerase II-mediated transcriptional elongation and many
other processes, including cytoskeleton organization, exocytosis, and tRNA
modification. Here, we determined the crystal structure of the Elp4-6 subcomplex
of yeast. The overall structure of Elp4-6 revealed that Elp6 acts as a bridge to
assemble Elp4 and Elp5. Detailed structural and sequence analyses revealed that
each subunit in the Elp4-6 subcomplex forms a RecA-ATPase-like fold, although it
lacks the key sequence signature of ATPases. Site-directed mutagenesis and
biochemical analyses indicated that the Elp4-6 subcomplex can assemble into a
hexameric ring-shaped structure in vitro and in vivo. Furthermore, GST pulldown
assays showed that the ring-shaped assembly of the Elp4-6 subcomplex is
important for its specific histone H3 binding. Our results may shed light on the
substrate recognition and assembly of the holo-Elongator complex.
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