1XHZ

Phi29 DNA polymerase, orthorhombic crystal form, ssDNA complex

1XHZ の概要

• エントリーDOI: 10.2210/pdb1xhz/pdb
• 関連するPDBエントリー: 1XHX
• 分子名称: 5'-D(*TP*TP*TP*TP*T)-3', DNA polymerase (3 entities in total)
• 機能のキーワード: dna polymerase, protein-primed, strand displacement, processivity, replication, transferase-dna complex, transferase/dna
• 由来する生物種: Bacillus phage phi29
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 272787.68

構造登録者

Kamtekar, S.,Berman, A.J.,Wang, J.,Lazaro, J.M.,de Vega, M.,Blanco, L.,Salas, M.,Steitz, T.A. (登録日: 2004-09-21, 公開日: 2004-12-07, 最終更新日: 2024-02-14)

主引用文献

Kamtekar, S.,Berman, A.J.,Wang, J.,Lazaro, J.M.,de Vega, M.,Blanco, L.,Salas, M.,Steitz, T.A.
Insights into Strand Displacement and Processivity from the Crystal Structure of the Protein-Primed DNA Polymerase of Bacteriophage phi29
Mol.Cell, 16:609-618, 2004

PubMed Abstract: The DNA polymerase from phage phi29 is a B family polymerase that initiates replication using a protein as a primer, attaching the first nucleotide of the phage genome to the hydroxyl of a specific serine of the priming protein. The crystal structure of phi29 DNA polymerase determined at 2.2 A resolution provides explanations for its extraordinary processivity and strand displacement activities. Homology modeling suggests that downstream template DNA passes through a tunnel prior to entering the polymerase active site. This tunnel is too small to accommodate double-stranded DNA and requires the separation of template and nontemplate strands. Members of the B family of DNA polymerases that use protein primers contain two sequence insertions: one forms a domain not previously observed in polymerases, while the second resembles the specificity loop of T7 RNA polymerase. The high processivity of phi29 DNA polymerase may be explained by its topological encirclement of both the downstream template and the upstream duplex DNA.

PubMed: 15546620
DOI: 10.1016/j.molcel.2004.10.019

実験手法

X-RAY DIFFRACTION (2.7 Å)