2XUR
The G157C mutation in the Escherichia coli sliding clamp specifically affects initiation of replication
Summary for 2XUR
| Entry DOI | 10.2210/pdb2xur/pdb |
| Descriptor | DNA POLYMERASE III SUBUNIT BETA (2 entities in total) |
| Functional Keywords | replication, transferase, dna-directed dna polymerase |
| Biological source | ESCHERICHIA COLI |
| Cellular location | Cytoplasm: P0A988 |
| Total number of polymer chains | 2 |
| Total formula weight | 83273.34 |
| Authors | Johnsen, L.,Morigen,Dalhus, B.,Bjoras, M.,Flaatten, I.,Waldminghaus, T.,Skarstad, K. (deposition date: 2010-10-20, release date: 2011-02-16, Last modification date: 2023-12-20) |
| Primary citation | Johnsen, L.,Flaatten, I.,Morigen,Dalhus, B.,Bjoras, M.,Waldminghaus, T.,Skarstad, K. The G157C Mutation in the Escherichia Coli Sliding Clamp Specifically Affects Initiation of Replication. Mol.Microbiol., 79:433-, 2011 Cited by PubMed Abstract: Escherichia coli cells with a point mutation in the dnaN gene causing the amino acid change Gly157 to Cys, were found to underinitiate replication and grow with a reduced origin and DNA concentration. The mutant β clamp also caused excessive conversion of ATP-DnaA to ADP-DnaA. The DnaA protein was, however, not the element limiting initiation of replication. Overproduction of DnaA protein, which in wild-type cells leads to over-replication, had no effect in the dnaN(G157C) mutant. Origins already opened by DnaA seemed to remain open for a prolonged period, with a stage of initiation involving β clamp loading, presumably limiting the initiation process. The existence of opened origins led to a moderate SOS response. Lagging strand synthesis, which also requires loading of the β clamp, was apparently unaffected. The result indicates that some aspects of β clamp activity are specific to the origin. It is possible that the origin specific activities of β contribute to regulation of initiation frequency. PubMed: 21219462DOI: 10.1111/J.1365-2958.2010.07453.X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report






