2RT6
Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain
Summary for 2RT6
| Entry DOI | 10.2210/pdb2rt6/pdb |
| NMR Information | BMRB: 11525 |
| Descriptor | Primosomal replication protein N'' (1 entity in total) |
| Functional Keywords | primosome, replication restart, pric, dna binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 11007.53 |
| Authors | Aramaki, T.,Abe, Y.,Katayama, T.,Ueda, T. (deposition date: 2013-04-24, release date: 2013-08-07, Last modification date: 2024-05-15) |
| Primary citation | Aramaki, T.,Abe, Y.,Katayama, T.,Ueda, T. Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli. Protein Sci., 22:1279-1286, 2013 Cited by PubMed Abstract: In eubacterial organisms, the oriC-independent primosome plays an essential role in replication restart after the dissociation of the replication DNA-protein complex by DNA damage. PriC is a key protein component in the replication restart primosome. Our recent study suggested that PriC is divided into two domains: an N-terminal and a C-terminal domain. In the present study, we determined the solution structure of the N-terminal domain, whose structure and function have remained unknown until now. The revealed structure was composed of three helices and one extended loop. We also observed chemical shift changes in the heteronuclear NMR spectrum and oligomerization in the presence of ssDNA. These abilities may contribute to the PriC-ssDNA complex, which is important for the replication restart primosome. PubMed: 23868391DOI: 10.1002/pro.2314 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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