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PDBsum entry 4c3i
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Contents |
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1484 a.a.
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1176 a.a.
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304 a.a.
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59 a.a.
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215 a.a.
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100 a.a.
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259 a.a.
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134 a.a.
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124 a.a.
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69 a.a.
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103 a.a.
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45 a.a.
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105 a.a.
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139 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 the 14-Subunit RNA polymerase i.
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Authors
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C.Fernández-Tornero,
M.Moreno-Morcillo,
U.J.Rashid,
N.M.Taylor,
F.M.Ruiz,
T.Gruene,
P.Legrand,
U.Steuerwald,
C.W.Müller.
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Ref.
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Nature, 2013,
502,
644-649.
[DOI no: ]
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PubMed id
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Abstract
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Protein biosynthesis depends on the availability of ribosomes, which in turn
relies on ribosomal RNA production. In eukaryotes, this process is carried out
by RNA polymerase I (Pol I), a 14-subunit enzyme, the activity of which is a
major determinant of cell growth. Here we present the crystal structure of Pol I
from Saccharomyces cerevisiae at 3.0 Å resolution. The Pol I structure shows
a compact core with a wide DNA-binding cleft and a tightly anchored stalk. An
extended loop mimics the DNA backbone in the cleft and may be involved in
regulating Pol I transcription. Subunit A12.2 extends from the A190 jaw to the
active site and inserts a transcription elongation factor TFIIS-like zinc ribbon
into the nucleotide triphosphate entry pore, providing insight into the role of
A12.2 in RNA cleavage and Pol I insensitivity to α-amanitin. The A49-A34.5
heterodimer embraces subunit A135 through extended arms, thereby contacting and
potentially regulating subunit A12.2.
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