4BPU
Crystal structure of human primase in heterodimeric form, comprising PriS and truncated PriL lacking the C-terminal Fe-S domain.
Summary for 4BPU
| Entry DOI | 10.2210/pdb4bpu/pdb |
| Related | 4BPW 4BPX |
| Descriptor | DNA PRIMASE SMALL SUBUNIT, DNA PRIMASE LARGE SUBUNIT, ZINC ION, ... (5 entities in total) |
| Functional Keywords | transferase, dna-dependent rna polymerase |
| Biological source | HOMO SAPIENS More |
| Total number of polymer chains | 4 |
| Total formula weight | 160279.59 |
| Authors | Kilkenny, M.L.,Perera, R.L.,Pellegrini, L. (deposition date: 2013-05-28, release date: 2013-09-25, Last modification date: 2024-05-08) |
| Primary citation | Kilkenny, M.L.,Longo, M.,Perera, R.L.,Pellegrini, L. Structures of Human Primase Reveal Design of Nucleotide Elongation Site and Mode of Pol Alpha Tethering Proc.Natl.Acad.Sci.USA, 110:15961-, 2013 Cited by PubMed Abstract: Initiation of DNA synthesis in genomic duplication depends on primase, the DNA-dependent RNA polymerase that synthesizes de novo the oligonucleotides that prime DNA replication. Due to the discontinuous nature of DNA replication, primase activity on the lagging strand is required throughout the replication process. In eukaryotic cells, the presence of primase at the replication fork is secured by its physical association with DNA polymerase α (Pol α), which extends the RNA primer with deoxynucleotides. Our knowledge of the mechanism that primes DNA synthesis is very limited, as structural information for the eukaryotic enzyme has proved difficult to obtain. Here, we describe the crystal structure of human primase in heterodimeric form consisting of full-length catalytic subunit and a C-terminally truncated large subunit. We exploit the crystallographic model to define the architecture of its nucleotide elongation site and to show that the small subunit integrates primer initiation and elongation within the same set of functional residues. Furthermore, we define in atomic detail the mode of association of primase to Pol α, the critical interaction that keeps primase tethered to the eukaryotic replisome. PubMed: 24043831DOI: 10.1073/PNAS.1311185110 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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