DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The beta chain is required for initiation of replication from an RNA primer, nucleotide triphosphate (dNTP) residues being added to the 5'-end of the growing DNA chain.
Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp.
Cell. 1992; 69: 425-37
Display abstract
The crystal structure of the beta subunit (processivity factor) of DNA polymerase III holoenzyme has been determined at 2.5 A resolution. A dimer of the beta subunit (M(r) = 2 x 40.6 kd, 2 x 366 amino acid residues) forms a ring-shaped structure lined by 12 alpha helices that can encircle duplex DNA. The structure is highly symmetrical, with each monomer containing three domains of identical topology. The charge distribution and orientation of the helices indicate that the molecule functions by forming a tight clamp that can slide on DNA, as shown biochemically. A potential structural relationship is suggested between the beta subunit and proliferating cell nuclear antigen (PCNA, the eukaryotic polymerase delta [and epsilon] processivity factor), and the gene 45 protein of the bacteriophage T4 DNA polymerase.
Metabolism (metabolic pathways involving proteins which contain this domain)
This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with POL3Bc domain which could be assigned to a KEGG orthologous group, and not all proteins containing POL3Bc domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of e. coli dna polymerase iii: structure of the beta-delta complex
Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of e. coli dna polymerase iii: structure of beta-delta (1-140)