2AVT

Crystal structure of the beta subunit from DNA polymerase of Streptococcus pyogenes


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.284 
  • R-Value Work: 0.245 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of a DNA polymerase sliding clamp from a Gram-positive bacterium.

Argiriadi, M.A.Goedken, E.R.Bruck, I.O'donnell, M.Kuriyan, J.

(2006) BMC Struct Biol 6: 2-2

  • DOI: https://doi.org/10.1186/1472-6807-6-2
  • Primary Citation of Related Structures:  
    2AVT

  • PubMed Abstract: 

    Sliding DNA clamps are processivity factors that are required for efficient DNA replication. DNA polymerases maintain proximity to nucleic acid templates by interacting with sliding clamps that encircle DNA and thereby link the polymerase enzyme to the DNA substrate. Although the structures of sliding clamps from Gram-negative bacteria (E. coli), eukaryotes, archaea, and T4-like bacteriophages are well-known, the structure of a sliding clamp from Gram-positive bacteria has not been reported previously.


  • Organizational Affiliation

    Howard Hughes Medical Institute, The Rockefeller University, New York, NY 10021, USA. maria.argiriadi@abbott.com


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DNA polymerase III beta subunit
A, B
378Streptococcus pyogenesMutation(s): 0 
EC: 2.7.7
UniProt
Find proteins for Q9EVR1 (Streptococcus pyogenes)
Explore Q9EVR1 
Go to UniProtKB:  Q9EVR1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9EVR1
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.284 
  • R-Value Work: 0.245 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.036α = 90
b = 74.666β = 118.57
c = 82.779γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
SCALEPACKdata scaling
CNSrefinement
HKL-2000data reduction
CNSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-01-24
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references