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- PDB-1pqv: RNA polymerase II-TFIIS complex -

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Basic information

Entry
Database: PDB / ID: 1pqv
TitleRNA polymerase II-TFIIS complex
Components
  • (DNA-directed RNA polymerase II ...Polymerase) x 7
  • (DNA-directed RNA polymerases I, II, and III ...RNA polymerase) x 5
  • Transcription elongation factor S-II
KeywordsTRANSFERASE/TRANSCRIPTION / TRANSCRIPTION / MRNA CLEAVAGE / PROOFREADING / BACKTRACKING / GENE EXPRESSION / MULTIPROTEIN COMPLEX / PROTEIN SOAKING / TRANSFERASE-TRANSCRIPTION COMPLEX
Function / homology
Function and homology information


regulation of mRNA 3'-end processing / RNA polymerase II complex recruiting activity / transcription elongation from RNA polymerase I promoter / nuclear-transcribed mRNA catabolic process, exonucleolytic / recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex / mRNA export from nucleus in response to heat stress / RNA Polymerase I Transcription Initiation / RNA Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening ...regulation of mRNA 3'-end processing / RNA polymerase II complex recruiting activity / transcription elongation from RNA polymerase I promoter / nuclear-transcribed mRNA catabolic process, exonucleolytic / recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex / mRNA export from nucleus in response to heat stress / RNA Polymerase I Transcription Initiation / RNA Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase II promoter / termination of RNA polymerase II transcription / RNA Pol II CTD phosphorylation and interaction with CE / mRNA Capping / Formation of the Early Elongation Complex / RNA polymerase II transcribes snRNA genes / RNA Polymerase I Promoter Escape / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Promoter Escape / RNA polymerase II activity / RNA polymerase II complex binding / RNA polymerase I activity / RNA Polymerase II Transcription Elongation / positive regulation of translational initiation / Estrogen-dependent gene expression / Gap-filling DNA repair synthesis and ligation in TC-NER / Formation of TC-NER Pre-Incision Complex / tRNA transcription by RNA polymerase III / RNA Polymerase II Pre-transcription Events / Dual incision in TC-NER / transcription by RNA polymerase I / transcription-coupled nucleotide-excision repair / transcription by RNA polymerase III / mRNA cleavage / RNA polymerase I complex / RNA polymerase III complex / translesion synthesis / RNA polymerase II, core complex / transcription elongation from RNA polymerase II promoter / transcription antitermination / transcription initiation from RNA polymerase II promoter / translation initiation factor binding / positive regulation of transcription elongation from RNA polymerase II promoter / positive regulation of RNA polymerase II transcription preinitiation complex assembly / P-body / ribonucleoside binding / transcription by RNA polymerase II / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / RNA polymerase II transcription regulatory region sequence-specific DNA binding / transcription, RNA-templated / cytoplasmic stress granule / single-stranded DNA binding / ribosome biogenesis / single-stranded RNA binding / nucleic acid binding / protein dimerization activity / mRNA binding / nucleotide binding / nucleolus / negative regulation of transcription by RNA polymerase II / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / metal ion binding / nucleus / cytoplasm
Similarity search - Function
Transcription elongation factor, IIS-type / Transcription elongation factor, TFIIS / Domain in the central regions of transcription elongation factor S-II (and elsewhere) / Transcription factor S-II (TFIIS), central domain / TFIIS central domain profile. / Transcription elongation factor S-II, central domain / Transcription elongation factor S-II, central domain superfamily / Domain in the N-terminus of transcription elongation factor S-II (and elsewhere) / Transcription elongation factor, TFIIS/CRSP70, N-terminal, sub-type / TFIIS helical bundle-like domain ...Transcription elongation factor, IIS-type / Transcription elongation factor, TFIIS / Domain in the central regions of transcription elongation factor S-II (and elsewhere) / Transcription factor S-II (TFIIS), central domain / TFIIS central domain profile. / Transcription elongation factor S-II, central domain / Transcription elongation factor S-II, central domain superfamily / Domain in the N-terminus of transcription elongation factor S-II (and elsewhere) / Transcription elongation factor, TFIIS/CRSP70, N-terminal, sub-type / TFIIS helical bundle-like domain / Transcription factor IIS, N-terminal / TFIIS N-terminal domain profile. / TFIIS/LEDGF domain superfamily / DNA-directed RNA-polymerase II subunit / RNA polymerase Rpb4/RPC9, core / RNA polymerase II, heptapeptide repeat, eukaryotic / Eukaryotic RNA polymerase II heptapeptide repeat. / RNA polymerase Rpb1 C-terminal repeat / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb1, domain 7 / RNA polymerase Rpb1, domain 7 / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb1, domain 7 superfamily / Pol II subunit B9, C-terminal zinc ribbon / RNA polymerase RBP11 / RNA polymerase subunit Rpb4/RPC9 / RNA polymerase Rpb4 / RNA polymerase Rpb7-like , N-terminal / SHS2 domain found in N terminus of Rpb7p/Rpc25p/MJ0397 / HRDC-like superfamily / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb7-like, N-terminal domain superfamily / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 5 / Zinc finger TFIIS-type signature. / RNA polymerases N / 8 kDa subunit / RNA polymerase subunit RPB10 / DNA-directed RNA polymerase subunit RPABC5/Rpb10 / RNA polymerases, subunit N, zinc binding site / RNA polymerases N / 8 Kd subunits signature. / RNA polymerases M/15 Kd subunit / RNA polymerase subunit 9 / DNA-directed RNA polymerase, M/15kDa subunit / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / RNA polymerases M / 15 Kd subunits signature. / DNA-directed RNA polymerase M, 15kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo5/Rpb5 / RNA polymerase Rpb5, N-terminal domain superfamily / RNA polymerase, Rpb5, N-terminal / DNA-directed RNA polymerase subunit/transcription factor S / RNA polymerase Rpb5, N-terminal domain / RNA polymerase, Rpb8 / RNA polymerase subunit 8 / RNA polymerase Rpb8 / DNA-directed RNA polymerase, subunit RPB6 / DNA directed RNA polymerase, 7 kDa subunit / RNA polymerase archaeal subunit P/eukaryotic subunit RPABC4 / RNA polymerase subunit CX / RNA polymerases D / 30 to 40 Kd subunits signature. / DNA-directed RNA polymerase, 30-40kDa subunit, conserved site / RPB5-like RNA polymerase subunit superfamily / RNA polymerase Rpb5, C-terminal domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / : / RNA polymerases H / 23 Kd subunits signature. / RNA polymerases L / 13 to 16 Kd subunits signature. / RNA polymerase, subunit H/Rpb5 C-terminal / : / RNA polymerase, subunit H/Rpb5, conserved site / DNA-directed RNA polymerase Rpb11, 13-16kDa subunit, conserved site / DNA-directed RNA polymerase, RBP11-like dimerisation domain / RNA polymerases K / 14 to 18 Kd subunits signature. / Archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit / DNA-directed RNA polymerase, 14-18kDa subunit, conserved site / RNA polymerase subunit RPABC4/transcription elongation factor Spt4 / Transcription factor S-II (TFIIS) / Zinc finger, TFIIS-type / Zinc finger TFIIS-type profile. / C2C2 Zinc finger / Ribosomal protein S1-like RNA-binding domain / RNA-binding domain, S1 / S1 RNA binding domain / S1 domain / RNA polymerase Rpb1, domain 3 superfamily / RNA polymerase Rpb6 / RPB6/omega subunit-like superfamily / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / : / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 1 / RNA polymerase, N-terminal / RNA polymerase I subunit A N-terminus / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 4
Similarity search - Domain/homology
DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerase II subunit RPB11 / DNA-directed RNA polymerase II subunit RPB7 / DNA-directed RNA polymerase II subunit RPB9 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerase II subunit RPB4 / DNA-directed RNA polymerase II subunit RPB2 ...DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerase II subunit RPB11 / DNA-directed RNA polymerase II subunit RPB7 / DNA-directed RNA polymerase II subunit RPB9 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerase II subunit RPB4 / DNA-directed RNA polymerase II subunit RPB2 / Transcription elongation factor S-II / DNA-directed RNA polymerase II subunit RPB1 / DNA-directed RNA polymerases I, II, and III subunit RPABC4
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (baker's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.8 Å
AuthorsKettenberger, H. / Armache, K.-J. / Cramer, P.
Citation
Journal: Cell(Cambridge,Mass.) / Year: 2003
Title: Architecture of the RNA Polymerase II-TFIIS Complex and Implications for mRNA Cleavage
Authors: Kettenberger, H. / Armache, K.-J. / Cramer, P.
#1: Journal: Proc.Natl.Acad.Sci.USA / Year: 2003
Title: Architecture of initiation-competent 12-subunit RNA polymerase II
Authors: Armache, K.-J. / Kettenberger, H. / Cramer, P.
History
DepositionJun 19, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 19, 2003Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DNA-directed RNA polymerase II largest subunit
B: DNA-directed RNA polymerase II 140 kDa polypeptide
C: DNA-directed RNA polymerase II 45 kDa polypeptide
D: DNA-directed RNA polymerase II 32 kDa polypeptide
E: DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide
F: DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide
G: DNA-directed RNA polymerase II 19 kDa polypeptide
H: DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide
I: DNA-directed RNA polymerase II 14.2 kDa polypeptide
J: DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide
K: DNA-directed RNA polymerase II 13.6 kDa polypeptide
L: DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide
S: Transcription elongation factor S-II
hetero molecules


Theoretical massNumber of molelcules
Total (without water)548,89823
Polymers548,28513
Non-polymers61310
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)218.9, 395.3, 281.0
Angle α, β, γ (deg.)90, 90, 90
Int Tables number20
Cell settingorthorhombic
Space group name H-MC2221

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Components

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DNA-directed RNA polymerase II ... , 7 types, 7 molecules ABCDGIK

#1: Protein DNA-directed RNA polymerase II largest subunit / E.C.2.7.7.6 / B220 / Coordinate model: Cα atoms only


Mass: 191821.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P04050, DNA-directed RNA polymerase
#2: Protein DNA-directed RNA polymerase II 140 kDa polypeptide / E.C.2.7.7.6 / B150 / RNA polymerase II subunit 2 / Coordinate model: Cα atoms only


Mass: 138937.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P08518, DNA-directed RNA polymerase
#3: Protein DNA-directed RNA polymerase II 45 kDa polypeptide / E.C.2.7.7.6 / B44.5 / Coordinate model: Cα atoms only


Mass: 35330.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P16370, DNA-directed RNA polymerase
#4: Protein DNA-directed RNA polymerase II 32 kDa polypeptide / E.C.2.7.7.6 / B32 / Coordinate model: Cα atoms only


Mass: 24674.189 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P20433, DNA-directed RNA polymerase
#7: Protein DNA-directed RNA polymerase II 19 kDa polypeptide / E.C.2.7.7.6 / B16 / Coordinate model: Cα atoms only


Mass: 19081.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P34087, DNA-directed RNA polymerase
#9: Protein DNA-directed RNA polymerase II 14.2 kDa polypeptide / E.C.2.7.7.6 / B12.6 / Coordinate model: Cα atoms only


Mass: 14308.161 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P27999, DNA-directed RNA polymerase
#11: Protein DNA-directed RNA polymerase II 13.6 kDa polypeptide / E.C.2.7.7.6 / B13.6 / Coordinate model: Cα atoms only


Mass: 13633.493 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P38902, DNA-directed RNA polymerase

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DNA-directed RNA polymerases I, II, and III ... , 5 types, 5 molecules EFHJL

#5: Protein DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide / RNA polymerase / E.C.2.7.7.6 / ABC27 / Coordinate model: Cα atoms only


Mass: 25117.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P20434, DNA-directed RNA polymerase
#6: Protein DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide / RNA polymerase / E.C.2.7.7.6 / ABC23 / Coordinate model: Cα atoms only


Mass: 17931.834 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P20435, DNA-directed RNA polymerase
#8: Protein DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide / RNA polymerase / E.C.2.7.7.6 / ABC14.4 / Coordinate model: Cα atoms only


Mass: 16525.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P20436, DNA-directed RNA polymerase
#10: Protein DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide / RNA polymerase / E.C.2.7.7.6 / ABC10-beta / ABC8 / Coordinate model: Cα atoms only


Mass: 8290.732 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P22139, DNA-directed RNA polymerase
#12: Protein DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide / RNA polymerase / E.C.2.7.7.6 / ABC10-alpha / Coordinate model: Cα atoms only


Mass: 7729.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P40422, DNA-directed RNA polymerase

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Protein , 1 types, 1 molecules S

#13: Protein Transcription elongation factor S-II / DNA strand transfer protein alpha / STP-alpha / DNA strand transferase 1 / Pyrimidine pathway ...DNA strand transfer protein alpha / STP-alpha / DNA strand transferase 1 / Pyrimidine pathway regulatory protein 2 / Coordinate model: Cα atoms only


Mass: 34903.551 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / References: UniProt: P07273

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Non-polymers , 2 types, 10 molecules

#14: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#15: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Zn

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Details

Sequence detailsSEQUENCE Numbering of residues D86-D114 is arbitrary.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 5.54 Å3/Da / Density % sol: 77.81 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Crystal grow
*PLUS
Temperature: 20 ℃ / Method: vapor diffusion, sitting drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
14 mg/mlprotein1drop
2850 mMammonium-sodium tartrate1reservoir
3100 mMHEPES1reservoirpH7.5
45 mMdithiothreitol1reservoir

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.979 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Mar 26, 2003
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 3.8→50 Å / Num. all: 115508 / Num. obs: 115508 / % possible obs: 96.2 % / Observed criterion σ(I): -3 / Redundancy: 2.9 % / Rsym value: 0.089
Reflection shellResolution: 3.8→3.94 Å / Redundancy: 1.2 % / Num. unique all: 9618 / Rsym value: 0.355 / % possible all: 81
Reflection
*PLUS
Highest resolution: 3.8 Å / Rmerge(I) obs: 0.089
Reflection shell
*PLUS
Highest resolution: 3.8 Å / % possible obs: 81 % / Num. unique obs: 9618 / Rmerge(I) obs: 0.355 / Mean I/σ(I) obs: 1.9

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Processing

Software
NameClassification
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
Omodel building
CNSrefinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.8→50 Å / σ(F): 0 / Details: No least square refinement has been performed. /
Num. reflection% reflection
all115508 -
obs115508 96.2 %
Refinement stepCycle: LAST / Resolution: 3.8→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4031 0 10 0 4041
Refinement
*PLUS
Highest resolution: 3.8 Å / Rfactor Rwork: 0.392
Solvent computation
*PLUS
Displacement parameters
*PLUS

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