3LX1
Crystal Structure analysis of PCNA1 from Thermococcus kodakaraensis tk0535
Summary for 3LX1
| Entry DOI | 10.2210/pdb3lx1/pdb |
| Related | 3LX2 |
| Descriptor | DNA polymerase sliding clamp 1, SULFATE ION (3 entities in total) |
| Functional Keywords | pcna, dna processivity factor, trimer, toroidal, dna replication, dna-binding, dna binding protein |
| Biological source | Thermococcus kodakarensis (Thermococcus kodakaraensis) |
| Total number of polymer chains | 1 |
| Total formula weight | 29387.50 |
| Authors | Ladner, J.E.,Kelman, Z.,Pan, M. (deposition date: 2010-02-24, release date: 2011-01-26, Last modification date: 2024-02-21) |
| Primary citation | Ladner, J.E.,Pan, M.,Hurwitz, J.,Kelman, Z. Crystal structures of two active proliferating cell nuclear antigens (PCNAs) encoded by Thermococcus kodakaraensis. Proc.Natl.Acad.Sci.USA, 108:2711-2716, 2011 Cited by PubMed Abstract: Proliferating cell nuclear antigen (PCNA) is a ring-shaped protein that encircles duplex DNA and plays an essential role in many DNA metabolic processes in archaea and eukarya. The eukaryotic and euryarchaea genomes contain a single gene encoding for PCNA. Interestingly, the genome of the euryarchaeon Thermococcus kodakaraensis contains two PCNA-encoding genes (TK0535 and TK0582), making it unique among the euryarchaea kingdom. It is shown here that the two T. kodakaraensis PCNA proteins support processive DNA synthesis by the polymerase. Both proteins form trimeric structures with characteristics similar to those of other archaeal and eukaryal PCNA proteins. One of the notable differences between the TK0535 and TK0582 rings is that the interfaces are different, resulting in different stabilities for the two trimers. The possible implications of these observations for PCNA functions are discussed. PubMed: 21270332DOI: 10.1073/pnas.1019179108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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