4BPW

Crystal structure of human primase bound to UTP

4BPW の概要

• エントリーDOI: 10.2210/pdb4bpw/pdb
• 関連するPDBエントリー: 4BPU 4BPX
• 分子名称: DNA PRIMASE SMALL SUBUNIT, DNA PRIMASE LARGE SUBUNIT, ZINC ION, ... (5 entities in total)
• 機能のキーワード: transferase, dna-dependent rna polymerase, dna replication
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 160976.71

構造登録者

Kilkenny, M.L.,Perera, R.L.,Pellegrini, L. (登録日: 2013-05-28, 公開日: 2013-09-25, 最終更新日: 2024-05-08)

主引用文献

Kilkenny, M.L.,Longo, M.A.,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

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: 24043831
DOI: 10.1073/PNAS.1311185110

実験手法

X-RAY DIFFRACTION (3.003 Å)