| Literature DB >> 24637758 |
Andrey G Baranovskiy1, Jianyou Gu1, Nigar D Babayeva1, Vinod B Agarkar1, Yoshiaki Suwa1, Tahir H Tahirov1.
Abstract
Human primase synthesizes RNA primers and transfers them to the active site of Pol α with subsequent extension with dNTPs. Human primase is a heterodimer of two subunits: a small catalytic subunit (p49) and a large subunit (p58). The structural details of the initiation and elongation steps of primer synthesis, as well as primer length counting, are not known. To address these questions, structural studies of human primase were initiated. Two types of crystals were obtained. The best diffracting crystals belonged to space group P1, with unit-cell parameters a = 86.2, b = 88.9, c = 94.68 Å, α = 93.82, β = 96.57, γ = 111.72°, and contained two heterodimers of full-length p49 and p59 subunits in the asymmetric unit.Entities:
Keywords: DNA replication; human DNA primase; p49 subunit; p58 subunit
Mesh:
Substances:
Year: 2014 PMID: 24637758 PMCID: PMC3936435 DOI: 10.1107/S2053230X13034432
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056