2WAQ

The complete structure of the archaeal 13-subunit DNA-directed RNA Polymerase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.35 Å
  • R-Value Free: 0.341 
  • R-Value Work: 0.271 
  • R-Value Observed: 0.274 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


This is version 1.7 of the entry. See complete history


Literature

Evolution of complex RNA polymerases: the complete archaeal RNA polymerase structure.

Korkhin, Y.Unligil, U.M.Littlefield, O.Nelson, P.J.Stuart, D.I.Sigler, P.B.Bell, S.D.Abrescia, N.G.

(2009) PLoS Biol 7: e1000102-e1000102

  • DOI: https://doi.org/10.1371/journal.pbio.1000102
  • Primary Citation of Related Structures:  
    2WAQ, 2WB1

  • PubMed Abstract: 

    The archaeal RNA polymerase (RNAP) shares structural similarities with eukaryotic RNAP II but requires a reduced subset of general transcription factors for promoter-dependent initiation. To deepen our knowledge of cellular transcription, we have determined the structure of the 13-subunit DNA-directed RNAP from Sulfolobus shibatae at 3.35 Å resolution. The structure contains the full complement of subunits, including RpoG/Rpb8 and the equivalent of the clamp-head and jaw domains of the eukaryotic Rpb1. Furthermore, we have identified subunit Rpo13, an RNAP component in the order Sulfolobales, which contains a helix-turn-helix motif that interacts with the RpoH/Rpb5 and RpoA'/Rpb1 subunits. Its location and topology suggest a role in the formation of the transcription bubble.


  • Organizational Affiliation

    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO1N SUBUNIT880Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
UniProt
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO2 SUBUNIT1,131Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
UniProt
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO1C SUBUNIT395Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
UniProt
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO3 SUBUNIT265Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
UniProt
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO7 SUBUNIT180Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
UniProt
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO4 SUBUNIT113Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
UniProt
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO8 SUBUNIT132Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
UniProt
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO5 SUBUNIT84Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO6 SUBUNITI [auth K]95Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
UniProt
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Entity ID: 10
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO11 SUBUNITJ [auth L]92Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
UniProt
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Entity ID: 11
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO10 SUBUNITK [auth N]66Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
UniProt
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Entity ID: 12
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO12 SUBUNITL [auth P]48Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
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Entity ID: 13
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-DIRECTED RNA POLYMERASE RPO13 SUBUNITM [auth Q]104Saccharolobus shibataeMutation(s): 0 
EC: 2.7.7.6
UniProt
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Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
F3S
Query on F3S

Download Ideal Coordinates CCD File 
V [auth D]FE3-S4 CLUSTER
Fe3 S4
FCXHZBQOKRZXKS-UHFFFAOYSA-N
ZN
Query on ZN

Download Ideal Coordinates CCD File 
N [auth A]
O [auth A]
P [auth A]
R [auth B]
S [auth B]
N [auth A],
O [auth A],
P [auth A],
R [auth B],
S [auth B],
T [auth B],
U [auth C],
W [auth N],
X [auth P]
ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
MG
Query on MG

Download Ideal Coordinates CCD File 
Q [auth A]MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.35 Å
  • R-Value Free: 0.341 
  • R-Value Work: 0.271 
  • R-Value Observed: 0.274 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 193.501α = 90
b = 212.62β = 90
c = 128.998γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
SCALEPACKdata scaling
GLRFphasing
MOLREPphasing
SOLVEphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-05-19
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-01-30
    Changes: Data collection, Database references, Experimental preparation
  • Version 1.4: 2019-08-28
    Changes: Data collection, Database references
  • Version 1.5: 2021-04-28
    Changes: Data collection, Derived calculations, Other
  • Version 1.6: 2023-12-13
    Changes: Data collection, Database references, Refinement description
  • Version 1.7: 2024-11-13
    Changes: Structure summary