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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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References listed in PDB file
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Key reference
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Title
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Crystal structure of elongator subcomplex elp4-6.
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Authors
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Z.Lin,
W.Zhao,
W.Diao,
X.Xie,
Z.Wang,
J.Zhang,
Y.Shen,
J.Long.
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Ref.
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J Biol Chem, 2012,
287,
21501-21508.
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PubMed id
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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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