1PLQ
CRYSTAL STRUCTURE OF THE EUKARYOTIC DNA POLYMERASE PROCESSIVITY FACTOR PCNA
Summary for 1PLQ
| Entry DOI | 10.2210/pdb1plq/pdb |
| Descriptor | PROLIFERATING CELL NUCLEAR ANTIGEN (PCNA), MERCURY (II) ION (3 entities in total) |
| Functional Keywords | dna-binding, nuclear protein, dna replication, processivity factor |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Nucleus: P15873 |
| Total number of polymer chains | 1 |
| Total formula weight | 29345.23 |
| Authors | Krishna, T.S.R.,Kong, X.-P.,Gary, S.,Burgers, P.M.,Kuriyan, J. (deposition date: 1995-01-02, release date: 1995-03-31, Last modification date: 2024-02-14) |
| Primary citation | Krishna, T.S.,Kong, X.P.,Gary, S.,Burgers, P.M.,Kuriyan, J. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell(Cambridge,Mass.), 79:1233-1243, 1994 Cited by PubMed Abstract: The crystal structure of the processivity factor required by eukaryotic DNA polymerase delta, proliferating cell nuclear antigen (PCNA) from S. cerevisiae, has been determined at 2.3 A resolution. Three PCNA molecules, each containing two topologically identical domains, are tightly associated to form a closed ring. The dimensions and electrostatic properties of the ring suggest that PCNA encircles duplex DNA, providing a DNA-bound platform for the attachment of the polymerase. The trimeric PCNA ring is strikingly similar to the dimeric ring formed by the beta subunit (processivity factor) of E. coli DNA polymerase III holoenzyme, with which it shares no significant sequence identity. This structural correspondence further substantiates the mechanistic connection between eukaryotic and prokaryotic DNA replication that has been suggested on biochemical grounds. PubMed: 8001157DOI: 10.1016/0092-8674(94)90014-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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