4K74
The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.
Summary for 4K74
| Entry DOI | 10.2210/pdb4k74/pdb |
| Descriptor | DNA polymerase III subunit beta, UmuC peptide (3 entities in total) |
| Functional Keywords | dna replication clamp processivity factor, dna replication/repair, dna binding protein-transferase complex, dna binding protein/transferase |
| Biological source | Escherichia coli More |
| Cellular location | Cytoplasm (By similarity): Q1R4N6 |
| Total number of polymer chains | 4 |
| Total formula weight | 85563.65 |
| Authors | Patoli, A.A.,Winter, J.A.,Bunting, K.A. (deposition date: 2013-04-16, release date: 2013-07-17, Last modification date: 2023-09-20) |
| Primary citation | Patoli, A.A.,Winter, J.A.,Bunting, K.A. The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor. Bmc Struct.Biol., 13:12-12, 2013 Cited by PubMed Abstract: Strict regulation of replisome components is essential to ensure the accurate transmission of the genome to the next generation. The sliding clamp processivity factors play a central role in this regulation, interacting with both DNA polymerases and multiple DNA processing and repair proteins. Clamp binding partners share a common peptide binding motif, the nature of which is essentially conserved from phage through to humans. Given the degree of conservation of these motifs, much research effort has focussed on understanding how the temporal and spatial regulation of multiple clamp binding partners is managed. The bacterial sliding clamps have come under scrutiny as potential targets for rational drug design and comprehensive understanding of the structural basis of their interactions is crucial for success. PubMed: 23822808DOI: 10.1186/1472-6807-13-12 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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