1RO2

Bifunctional DNA primase/polymerase domain of ORF904 from the archaeal plasmid pRN1- Triple mutant F50M/L107M/L110M manganese soak

1RO2 の概要

• エントリーDOI: 10.2210/pdb1ro2/pdb
• 関連するPDBエントリー: 1RNI 1RO0
• 分子名称: hypothetical protein ORF904, ZINC ION, MANGANESE (II) ION, ... (4 entities in total)
• 機能のキーワード: dna polymerase, primase, replication, polymerization, evolution of nucleic acid polymerizing enzymes
• 由来する生物種: Sulfolobus islandicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25295.60

構造登録者

Lipps, G.,Weinzierl, A.O.,von Scheven, G.,Buchen, C.,Cramer, P. (登録日: 2003-12-01, 公開日: 2004-01-27, 最終更新日: 2024-10-30)

主引用文献

Lipps, G.,Weinzierl, A.O.,Von Scheven, G.,Buchen, C.,Cramer, P.
Structure of a bifunctional DNA primase-polymerase
Nat.Struct.Mol.Biol., 11:157-162, 2004

PubMed Abstract: Genome replication generally requires primases, which synthesize an initial oligonucleotide primer, and DNA polymerases, which elongate the primer. Primase and DNA polymerase activities are combined, however, in newly identified replicases from archaeal plasmids, such as pRN1 from Sulfolobus islandicus. Here we present a structure-function analysis of the pRN1 primase-polymerase (prim-pol) domain. The crystal structure shows a central depression lined by conserved residues. Mutations on one side of the depression reduce DNA affinity. On the opposite side of the depression cluster three acidic residues and a histidine, which are required for primase and DNA polymerase activity. One acidic residue binds a manganese ion, suggestive of a metal-dependent catalytic mechanism. The structure does not show any similarity to DNA polymerases, but is distantly related to archaeal and eukaryotic primases, with corresponding active-site residues. We propose that archaeal and eukaryotic primases and the prim-pol domain have a common evolutionary ancestor, a bifunctional replicase for small DNA genomes.

PubMed: 14730355
DOI: 10.1038/nsmb723

実験手法

X-RAY DIFFRACTION (1.6 Å)