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1442 a.a.
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1153 a.a.
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271 a.a.
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215 a.a.
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85 a.a.
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136 a.a.
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119 a.a.
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65 a.a.
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114 a.a.
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46 a.a.
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* Residue conservation analysis
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PDB id:
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Transcription, transferase/DNA-RNA hybri
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Title:
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Backtracked RNA polymerase ii complex with 18mer RNA
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Structure:
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DNA-directed RNA polymerase ii subunit rpb1. Chain: a. Fragment: DNA-directed RNA polymerase ii largest subunit. Synonym: RNA polymerase ii subunit b1, RNA polymerase ii subunit 1, DNA-directed RNA polymerase iii largest subunit, RNA polymerase ii subunit b220. DNA-directed RNA polymerase ii subunit rpb2. Chain: b. Fragment: DNA-directed RNA polymerase ii 140 kda polypeptide.
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Source:
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Saccharomyces cerevisiae. Yeast. Organism_taxid: 4932. Synthetic: yes. Other_details: synthetic RNA. Other_details: synthetic template DNA. Other_details: synthetic non-template DNA
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Resolution:
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3.80Å
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R-factor:
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0.248
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R-free:
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0.278
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Authors:
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D.Wang,D.A.Bushnell,X.Huang,K.D.Westover,M.Levitt,R.D.Kornberg
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Key ref:
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D.Wang
et al.
(2009).
Structural basis of transcription: backtracked RNA polymerase II at 3.4 angstrom resolution.
Science,
324,
1203-1206.
PubMed id:
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Date:
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27-Mar-09
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Release date:
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09-Jun-09
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PROCHECK
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Headers
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References
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P04050
(RPB1_YEAST) -
DNA-directed RNA polymerase II subunit RPB1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq: Struc:
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1733 a.a.
1442 a.a.
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P08518
(RPB2_YEAST) -
DNA-directed RNA polymerase II subunit RPB2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq: Struc:
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1224 a.a.
1153 a.a.
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P16370
(RPB3_YEAST) -
DNA-directed RNA polymerase II subunit RPB3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq: Struc:
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318 a.a.
271 a.a.
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P20434
(RPAB1_YEAST) -
DNA-directed RNA polymerases I, II, and III subunit RPABC1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq: Struc:
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215 a.a.
215 a.a.
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P20435
(RPAB2_YEAST) -
DNA-directed RNA polymerases I, II, and III subunit RPABC2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq: Struc:
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155 a.a.
85 a.a.
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P20436
(RPAB3_YEAST) -
DNA-directed RNA polymerases I, II, and III subunit RPABC3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq: Struc:
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146 a.a.
136 a.a.
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P27999
(RPB9_YEAST) -
DNA-directed RNA polymerase II subunit RPB9 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq: Struc:
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122 a.a.
119 a.a.
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P22139
(RPAB5_YEAST) -
DNA-directed RNA polymerases I, II, and III subunit RPABC5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq: Struc:
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70 a.a.
65 a.a.
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Enzyme class:
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Chains A, B:
E.C.2.7.7.6
- DNA-directed Rna polymerase.
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Reaction:
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RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
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RNA(n)
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+
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ribonucleoside 5'-triphosphate
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=
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RNA(n+1)
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+
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diphosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Science
324:1203-1206
(2009)
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PubMed id:
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Structural basis of transcription: backtracked RNA polymerase II at 3.4 angstrom resolution.
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D.Wang,
D.A.Bushnell,
X.Huang,
K.D.Westover,
M.Levitt,
R.D.Kornberg.
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ABSTRACT
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Transcribing RNA polymerases oscillate between three stable states, two of
which, pre- and posttranslocated, were previously subjected to x-ray crystal
structure determination. We report here the crystal structure of RNA polymerase
II in the third state, the reverse translocated, or "backtracked" state. The
defining feature of the backtracked structure is a binding site for the first
backtracked nucleotide. This binding site is occupied in case of nucleotide
misincorporation in the RNA or damage to the DNA, and is termed the "P" site
because it supports proofreading. The predominant mechanism of proofreading is
the excision of a dinucleotide in the presence of the elongation factor SII
(TFIIS). Structure determination of a cocrystal with TFIIS reveals a
rearrangement whereby cleavage of the RNA may take place.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.C.Cheung,
and
P.Cramer
(2011).
Structural basis of RNA polymerase II backtracking, arrest and reactivation.
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Nature,
471,
249-253.
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PDB codes:
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M.H.Larson,
R.Landick,
and
S.M.Block
(2011).
Single-molecule studies of RNA polymerase: one singular sensation, every little step it takes.
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Mol Cell,
41,
249-262.
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S.R.Kennedy,
and
D.A.Erie
(2011).
Templated nucleoside triphosphate binding to a noncatalytic site on RNA polymerase regulates transcription.
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Proc Natl Acad Sci U S A,
108,
6079-6084.
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D.Wang,
G.Zhu,
X.Huang,
and
S.J.Lippard
(2010).
X-ray structure and mechanism of RNA polymerase II stalled at an antineoplastic monofunctional platinum-DNA adduct.
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Proc Natl Acad Sci U S A,
107,
9584-9589.
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PDB codes:
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G.R.Bowman,
X.Huang,
and
V.S.Pande
(2010).
Network models for molecular kinetics and their initial applications to human health.
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Cell Res,
20,
622-630.
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G.Ruprich-Robert,
and
P.Thuriaux
(2010).
Non-canonical DNA transcription enzymes and the conservation of two-barrel RNA polymerases.
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Nucleic Acids Res,
38,
4559-4569.
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H.Koyama,
T.Ueda,
T.Ito,
and
K.Sekimizu
(2010).
Novel RNA polymerase II mutation suppresses transcriptional fidelity and oxidative stress sensitivity in rpb9Delta yeast.
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Genes Cells,
15,
151-159.
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J.Zhang,
M.Palangat,
and
R.Landick
(2010).
Role of the RNA polymerase trigger loop in catalysis and pausing.
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Nat Struct Mol Biol,
17,
99.
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N.Miropolskaya,
V.Nikiforov,
S.KlimaĊĦauskas,
I.Artsimovitch,
and
A.Kulbachinskiy
(2010).
Modulation of RNA polymerase activity through trigger loop folding.
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Transcr,
1,
89-94.
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P.P.Hein,
and
R.Landick
(2010).
The bridge helix coordinates movements of modules in RNA polymerase.
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BMC Biol,
8,
141.
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S.Sigurdsson,
A.B.Dirac-Svejstrup,
and
J.Q.Svejstrup
(2010).
Evidence that transcript cleavage is essential for RNA polymerase II transcription and cell viability.
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Mol Cell,
38,
202-210.
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S.Tagami,
S.Sekine,
T.Kumarevel,
N.Hino,
Y.Murayama,
S.Kamegamori,
M.Yamamoto,
K.Sakamoto,
and
S.Yokoyama
(2010).
Crystal structure of bacterial RNA polymerase bound with a transcription inhibitor protein.
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Nature,
468,
978-982.
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PDB codes:
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X.Huang,
D.Wang,
D.R.Weiss,
D.A.Bushnell,
R.D.Kornberg,
and
M.Levitt
(2010).
RNA polymerase II trigger loop residues stabilize and position the incoming nucleotide triphosphate in transcription.
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Proc Natl Acad Sci U S A,
107,
15745-15750.
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Y.Yuzenkova,
and
N.Zenkin
(2010).
Central role of the RNA polymerase trigger loop in intrinsic RNA hydrolysis.
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Proc Natl Acad Sci U S A,
107,
10878-10883.
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A.Hirata,
and
K.S.Murakami
(2009).
Archaeal RNA polymerase.
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Curr Opin Struct Biol,
19,
724-731.
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D.G.Vassylyev
(2009).
Elongation by RNA polymerase: a race through roadblocks.
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Curr Opin Struct Biol,
19,
691-700.
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J.F.Sydow,
F.Brueckner,
A.C.Cheung,
G.E.Damsma,
S.Dengl,
E.Lehmann,
D.Vassylyev,
and
P.Cramer
(2009).
Structural basis of transcription: mismatch-specific fidelity mechanisms and paused RNA polymerase II with frayed RNA.
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Mol Cell,
34,
710-721.
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PDB codes:
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N.Miropolskaya,
I.Artsimovitch,
S.Klimasauskas,
V.Nikiforov,
and
A.Kulbachinskiy
(2009).
Allosteric control of catalysis by the F loop of RNA polymerase.
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Proc Natl Acad Sci U S A,
106,
18942-18947.
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|
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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');
}
}
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