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2awa

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of DNA polymerase III, beta chain (EC 2.7.7.7) (np_344555.1) from STREPTOCOCCUS PNEUMONIAE TIGR4 at 2.50 A resolution. To be published
    Site JCSG
    PDB Id 2awa Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1397,NP_344555.1, _0106.000668_, 383214
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 4
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.76 Rfactor 0.192
    Waters
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    Solvent Content 55.16

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2awa
    1. Mutations in the Bacillus subtilis _ Clamp That Separate Its Roles in DNA Replication from Mismatch Repair
    NM Dupes, BW Walsh, AD Klocko - Journal of , 2010 - Am Soc Microbiol
     

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    Protein Summary

    The gene NP_344555.1 from Streptococcus pneumoniae encodes the N-terminal domain of the DNA polymerase III beta subunit (beta clamp domain) PF00712.  The enzyme catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time EC:2.7.7.7.  The beta subunit is required for initiation of replication from an RNA primer.  The protein belongs to the class of alpha and beta proteins (a+b) SCOP53931, and reveals DNA clamp fold type SCOP55978.  The beta subunit (processivity factor) of DNA polymerase III holoenzyme forms a ring shaped dimer that encircles dsDNA (sliding clamp) in bacteria. The beta-clamp is structurally similar to the trimeric ring formed by PCNA (Proliferating Cell Nuclear Antigen, found in eukaryotes and archaea) and the processivity factor (found in bacteriophages T4 and RB69).  To date, several structure of the enzyme homolgues from different organisms have been solved: 2AVTStreptococcus Pyogenes; 1OK7, E.coli; 1VPKThermotoga maritima.

    Ligand Summary



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