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Contents |
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1419 a.a.
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1094 a.a.
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266 a.a.
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215 a.a.
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84 a.a.
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133 a.a.
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122 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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| Name: |
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Transcription
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Title:
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RNA polymerase ii crystal form ii at 2.8 a resolution
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Structure:
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DNA-directed RNA polymerase ii largest subunit. Chain: a. Synonym: rpb1. DNA-directed RNA polymerase ii 140kd polypeptide. Chain: b. Synonym: rpb2. DNA-directed RNA polymerase ii 45kd polypeptide. Chain: c. Synonym: rpb3.
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Strain: delta-rpb4. Strain: delta-rpb4
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Biol. unit:
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Decamer (from
)
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Resolution:
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2.80Å
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R-factor:
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0.229
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R-free:
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0.282
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Authors:
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P.Cramer,D.A.Bushnell,R.D.Kornberg
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Key ref:
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P.Cramer
et al.
(2001).
Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution.
Science,
292,
1863-1876.
PubMed id:
DOI:
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Date:
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23-Feb-01
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Release date:
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23-Apr-01
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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
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|
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Seq: Struc:
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1733 a.a.
1419 a.a.
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P08518
(RPB2_YEAST) -
DNA-directed RNA polymerase II subunit RPB2
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Seq: Struc:
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1224 a.a.
1094 a.a.
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P16370
(RPB3_YEAST) -
DNA-directed RNA polymerase II subunit RPB3
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|
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Seq: Struc:
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318 a.a.
266 a.a.
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P20434
(RPAB1_YEAST) -
DNA-directed RNA polymerases I, II, and III subunit RPABC1
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|
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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
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|
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Seq: Struc:
|
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155 a.a.
84 a.a.
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P20436
(RPAB3_YEAST) -
DNA-directed RNA polymerases I, II, and III subunit RPABC3
|
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|
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Seq: Struc:
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146 a.a.
133 a.a.
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P27999
(RPB9_YEAST) -
DNA-directed RNA polymerase II subunit RPB9
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|
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Seq: Struc:
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122 a.a.
122 a.a.
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P22139
(RPAB5_YEAST) -
DNA-directed RNA polymerases I, II, and III subunit RPABC5
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|
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Seq: Struc:
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 |
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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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Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
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Nucleoside triphosphate
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+
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RNA(n)
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=
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diphosphate
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+
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RNA(n+1)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Cellular component
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RNA polymerase complex
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9 terms
|
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Biological process
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response to DNA damage stimulus
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10 terms
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Biochemical function
|
protein binding
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11 terms
|
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DOI no:
|
Science
292:1863-1876
(2001)
|
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PubMed id:
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| |
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Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution.
|
|
P.Cramer,
D.A.Bushnell,
R.D.Kornberg.
|
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|
| |
ABSTRACT
|
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| |
|
Structures of a 10-subunit yeast RNA polymerase II have been derived from two
crystal forms at 2.8 and 3.1 angstrom resolution. Comparison of the structures
reveals a division of the polymerase into four mobile modules, including a
clamp, shown previously to swing over the active center. In the 2.8 angstrom
structure, the clamp is in an open state, allowing entry of straight promoter
DNA for the initiation of transcription. Three loops extending from the clamp
may play roles in RNA unwinding and DNA rewinding during transcription. A 2.8
angstrom difference Fourier map reveals two metal ions at the active site, one
persistently bound and the other possibly exchangeable during RNA synthesis. The
results also provide evidence for RNA exit in the vicinity of the
carboxyl-terminal repeat domain, coupling synthesis to RNA processing by enzymes
bound to this domain.
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| |
Selected figure(s)
|
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| |
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|
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Figure 7.
Fig. 7. Four mobile modules of the Pol II structure. (A)
Backbone traces of the core, jaw-lobe, clamp, and shelf modules
of the form 1 structure, shown in gray, blue, yellow, and pink,
respectively. (B) Changes in the position of the jaw-lobe,
clamp, and shelf modules between form 1 (colored) and form 2
structures (gray). The arrows indicate the direction of charges
from form 1 to form 2. The core modules in the two crystal forms
were superimposed and then omitted for clarity. (C) The view in
(B) rotated 90° about a vertical axis. The core and jaw-lobe
modules are omitted for clarity. In form 2, the clamp has swung
to the left, opening a wider gap between its edge and the wall
located further to the right (not shown).
|
 |
Figure 8.
Fig. 8. Active center. Stereoview from the Rpb2 side toward the
clamp. Two metal ions are revealed in a [A]-weighted
mF[obs] DF[calc]
difference Fourier map (shown for metal B in green, contoured at
3.0 ) and in a
Mn2+ anomalous difference Fourier map (shown for metal A in
blue, contoured at 4.0 ). This
figure was prepared with BOBSCRIPT (85) and MOLSCRIPT (86).
|
 |
|
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|
| |
The above figures are
reprinted
by permission from the AAAs:
Science
(2001,
292,
1863-1876)
copyright 2001.
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| |
Figures were
selected
by the author.
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Literature references that cite this PDB file's key reference
|
|
 |
| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
A.Y.Park,
and
C.V.Robinson
(2011).
Protein-nucleic acid complexes and the role of mass spectrometry in their structure determination.
|
| |
Crit Rev Biochem Mol Biol, 46,
152-164.
|
 |
|
|
|
|
 |
E.Czeko,
M.Seizl,
C.Augsberger,
T.Mielke,
and
P.Cramer
(2011).
Iwr1 directs RNA polymerase II nuclear import.
|
| |
Mol Cell, 42,
261-266.
|
 |
|
|
|
|
 |
F.A.Rey,
and
W.I.Sundquist
(2011).
Macromolecular assemblages.
|
| |
Curr Opin Struct Biol, 21,
221-222.
|
 |
|
|
|
|
 |
F.W.Martinez-Rucobo,
S.Sainsbury,
A.C.Cheung,
and
P.Cramer
(2011).
Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity.
|
| |
EMBO J, 30,
1302-1310.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
F.Werner,
and
D.Grohmann
(2011).
Evolution of multisubunit RNA polymerases in the three domains of life.
|
| |
Nat Rev Microbiol, 9,
85-98.
|
 |
|
|
|
|
 |
J.N.Kuehner,
E.L.Pearson,
and
C.Moore
(2011).
Unravelling the means to an end: RNA polymerase II transcription termination.
|
| |
Nat Rev Mol Cell Biol, 12,
283-294.
|
 |
|
|
|
|
 |
J.Soutourina,
S.Wydau,
Y.Ambroise,
C.Boschiero,
and
M.Werner
(2011).
Direct interaction of RNA polymerase II and mediator required for transcription in vivo.
|
| |
Science, 331,
1451-1454.
|
 |
|
|
|
|
 |
L.A.Lane,
C.Fernández-Tornero,
M.Zhou,
N.Morgner,
D.Ptchelkine,
U.Steuerwald,
A.Politis,
D.Lindner,
J.Gvozdenovic,
A.C.Gavin,
C.W.Müller,
and
C.V.Robinson
(2011).
Mass spectrometry reveals stable modules in holo and apo RNA polymerases I and III.
|
| |
Structure, 19,
90.
|
 |
|
|
|
|
 |
M.H.Larson,
R.Landick,
and
S.M.Block
(2011).
Single-molecule studies of RNA polymerase: one singular sensation, every little step it takes.
|
| |
Mol Cell, 41,
249-262.
|
 |
|
|
|
|
 |
M.Wojtas,
B.Peralta,
M.Ondiviela,
M.Mogni,
S.D.Bell,
and
N.G.Abrescia
(2011).
Archaeal RNA polymerase: the influence of the protruding stalk in crystal packing and preliminary biophysical analysis of the Rpo13 subunit.
|
| |
Biochem Soc Trans, 39,
25-30.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
S.H.Jun,
M.J.Reichlen,
M.Tajiri,
and
K.S.Murakami
(2011).
Archaeal RNA polymerase and transcription regulation.
|
| |
Crit Rev Biochem Mol Biol, 46,
27-40.
|
 |
|
|
|
|
 |
S.Lefèvre,
H.Dumay-Odelot,
L.El-Ayoubi,
A.Budd,
P.Legrand,
N.Pinaud,
M.Teichmann,
and
S.Fribourg
(2011).
Structure-function analysis of hRPC62 provides insights into RNA polymerase III transcription initiation.
|
| |
Nat Struct Mol Biol, 18,
352-358.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
A.Tupin,
M.Gualtieri,
J.P.Leonetti,
and
K.Brodolin
(2010).
The transcription inhibitor lipiarmycin blocks DNA fitting into the RNA polymerase catalytic site.
|
| |
EMBO J, 29,
2527-2537.
|
 |
|
|
|
|
 |
C.Fernández-Tornero,
B.Böttcher,
U.J.Rashid,
U.Steuerwald,
B.Flörchinger,
D.P.Devos,
D.Lindner,
and
C.W.Müller
(2010).
Conformational flexibility of RNA polymerase III during transcriptional elongation.
|
| |
EMBO J, 29,
3762-3772.
|
 |
|
|
|
|
 |
C.Uetrecht,
R.J.Rose,
E.van Duijn,
K.Lorenzen,
and
A.J.Heck
(2010).
Ion mobility mass spectrometry of proteins and protein assemblies.
|
| |
Chem Soc Rev, 39,
1633-1655.
|
 |
|
|
|
|
 |
D.Elmlund,
R.Davis,
and
H.Elmlund
(2010).
Ab initio structure determination from electron microscopic images of single molecules coexisting in different functional states.
|
| |
Structure, 18,
777-786.
|
 |
|
|
|
|
 |
D.F.Kelly,
D.Dukovski,
and
T.Walz
(2010).
Strategy for the use of affinity grids to prepare non-His-tagged macromolecular complexes for single-particle electron microscopy.
|
| |
J Mol Biol, 400,
675-681.
|
 |
|
|
|
|
 |
D.Pupov,
N.Miropolskaya,
A.Sevostyanova,
I.Bass,
I.Artsimovitch,
and
A.Kulbachinskiy
(2010).
Multiple roles of the RNA polymerase {beta}' SW2 region in transcription initiation, promoter escape, and RNA elongation.
|
| |
Nucleic Acids Res, 38,
5784-5796.
|
 |
|
|
|
|
 |
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.
|
| |
Proc Natl Acad Sci U S A, 107,
9584-9589.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
G.A.Kassavetis,
P.Prakash,
and
E.Shim
(2010).
The C53/C37 subcomplex of RNA polymerase III lies near the active site and participates in promoter opening.
|
| |
J Biol Chem, 285,
2695-2706.
|
 |
|
|
|
|
 |
G.Ruprich-Robert,
and
P.Thuriaux
(2010).
Non-canonical DNA transcription enzymes and the conservation of two-barrel RNA polymerases.
|
| |
Nucleic Acids Res, 38,
4559-4569.
|
 |
|
|
|
|
 |
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.
|
| |
Genes Cells, 15,
151-159.
|
 |
|
|
|
|
 |
J.Eichner,
H.T.Chen,
L.Warfield,
and
S.Hahn
(2010).
Position of the general transcription factor TFIIF within the RNA polymerase II transcription preinitiation complex.
|
| |
EMBO J, 29,
706-716.
|
 |
|
|
|
|
 |
M.J.Muñoz,
M.de la Mata,
and
A.R.Kornblihtt
(2010).
The carboxy terminal domain of RNA polymerase II and alternative splicing.
|
| |
Trends Biochem Sci, 35,
497-504.
|
 |
|
|
|
|
 |
N.Visa,
and
P.Percipalle
(2010).
Nuclear functions of actin.
|
| |
Cold Spring Harb Perspect Biol, 2,
a000620.
|
 |
|
|
|
|
 |
P.Cramer
(2010).
Towards molecular systems biology of gene transcription and regulation.
|
| |
Biol Chem, 391,
731-735.
|
 |
|
|
|
|
 |
R.O.Weinzierl
(2010).
The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domain.
|
| |
BMC Biol, 8,
134.
|
 |
|
|
|
|
 |
S.Grünberg,
C.Reich,
M.E.Zeller,
M.S.Bartlett,
and
M.Thomm
(2010).
Rearrangement of the RNA polymerase subunit H and the lower jaw in archaeal elongation complexes.
|
| |
Nucleic Acids Res, 38,
1950-1963.
|
 |
|
|
|
|
 |
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.
|
| |
Nature, 468,
978-982.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
S.Y.Hong,
and
P.J.Chen
(2010).
Phosphorylation of serine 177 of the small hepatitis delta antigen regulates viral antigenomic RNA replication by interacting with the processive RNA polymerase II.
|
| |
J Virol, 84,
1430-1438.
|
 |
|
|
|
|
 |
T.J.Gries,
W.S.Kontur,
M.W.Capp,
R.M.Saecker,
and
M.T.Record
(2010).
One-step DNA melting in the RNA polymerase cleft opens the initiation bubble to form an unstable open complex.
|
| |
Proc Natl Acad Sci U S A, 107,
10418-10423.
|
 |
|
|
|
|
 |
T.Marcussen,
B.Oxelman,
A.Skog,
and
K.S.Jakobsen
(2010).
Evolution of plant RNA polymerase IV/V genes: evidence of subneofunctionalization of duplicated NRPD2/NRPE2-like paralogs in Viola (Violaceae).
|
| |
BMC Evol Biol, 10,
45.
|
 |
|
|
|
|
 |
W.J.Lane,
and
S.A.Darst
(2010).
Molecular evolution of multisubunit RNA polymerases: structural analysis.
|
| |
J Mol Biol, 395,
686-704.
|
 |
|
|
|
|
 |
W.J.Lane,
and
S.A.Darst
(2010).
Molecular evolution of multisubunit RNA polymerases: sequence analysis.
|
| |
J Mol Biol, 395,
671-685.
|
 |
|
|
|
|
 |
X.Li,
S.A.Hayik,
and
K.M.Merz
(2010).
QM/MM X-ray refinement of zinc metalloenzymes.
|
| |
J Inorg Biochem, 104,
512-522.
|
 |
|
|
|
|
 |
Z.A.Chen,
A.Jawhari,
L.Fischer,
C.Buchen,
S.Tahir,
T.Kamenski,
M.Rasmussen,
L.Lariviere,
J.C.Bukowski-Wills,
M.Nilges,
P.Cramer,
and
J.Rappsilber
(2010).
Architecture of the RNA polymerase II-TFIIF complex revealed by cross-linking and mass spectrometry.
|
| |
EMBO J, 29,
717-726.
|
 |
|
|
|
|
 |
Z.Dauter,
M.Jaskolski,
and
A.Wlodawer
(2010).
Impact of synchrotron radiation on macromolecular crystallography: a personal view.
|
| |
J Synchrotron Radiat, 17,
433-444.
|
 |
|
|
|
|
 |
A.Hirata,
and
K.S.Murakami
(2009).
Archaeal RNA polymerase.
|
| |
Curr Opin Struct Biol, 19,
724-731.
|
 |
|
|
|
|
 |
A.Korkut,
and
W.A.Hendrickson
(2009).
A force field for virtual atom molecular mechanics of proteins.
|
| |
Proc Natl Acad Sci U S A, 106,
15667-15672.
|
 |
|
|
|
|
 |
B.P.Hudson,
J.Quispe,
S.Lara-González,
Y.Kim,
H.M.Berman,
E.Arnold,
R.H.Ebright,
and
C.L.Lawson
(2009).
Three-dimensional EM structure of an intact activator-dependent transcription initiation complex.
|
| |
Proc Natl Acad Sci U S A, 106,
19830-19835.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
C.Reich,
M.Zeller,
P.Milkereit,
W.Hausner,
P.Cramer,
H.Tschochner,
and
M.Thomm
(2009).
The archaeal RNA polymerase subunit P and the eukaryotic polymerase subunit Rpb12 are interchangeable in vivo and in vitro.
|
| |
Mol Microbiol, 71,
989.
|
 |
|
|
|
|
 |
C.W.Carter
(2009).
E pluribus tres: the 2009 nobel prize in chemistry.
|
| |
Structure, 17,
1558-1561.
|
 |
|
|
|
|
 |
C.Walmacq,
M.L.Kireeva,
J.Irvin,
Y.Nedialkov,
L.Lubkowska,
F.Malagon,
J.N.Strathern,
and
M.Kashlev
(2009).
Rpb9 subunit controls transcription fidelity by delaying NTP sequestration in RNA polymerase II.
|
| |
J Biol Chem, 284,
19601-19612.
|
 |
|
|
|
|
 |
C.Y.Chen,
C.C.Chang,
C.F.Yen,
M.T.Chiu,
and
W.H.Chang
(2009).
Mapping RNA exit channel on transcribing RNA polymerase II by FRET analysis.
|
| |
Proc Natl Acad Sci U S A, 106,
127-132.
|
 |
|
|
|
|
 |
D.Kostrewa,
M.E.Zeller,
K.J.Armache,
M.Seizl,
K.Leike,
M.Thomm,
and
P.Cramer
(2009).
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Cell, 131,
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PDB code:
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Nature, 448,
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PDB code:
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Biol Direct, 2,
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Genome Biol, 8,
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J Virol, 81,
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PDB codes:
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M.W.Lee,
B.J.Kim,
H.K.Choi,
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PLoS Biol, 5,
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Structural confirmation of a bent and open model for the initiation complex of T7 RNA polymerase.
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Mol Cell Biol, 27,
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Structural biology of RNA polymerase III: subcomplex C17/25 X-ray structure and 11 subunit enzyme model.
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| |
Mol Cell, 23,
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|
PDB code:
|
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|
 |
A.Ujvári,
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| |
Cell, 127,
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|
 |
|
PDB codes:
|
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