2POL

THREE-DIMENSIONAL STRUCTURE OF THE BETA SUBUNIT OF ESCHERICHIA COLI DNA POLYMERASE III HOLOENZYME: A SLIDING DNA CLAMP

2POL の概要

• エントリーDOI: 10.2210/pdb2pol/pdb
• 分子名称: DNA POLYMERASE III (BETA SUBUNIT) (2 entities in total)
• 機能のキーワード: nucleotidyltransferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A988
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81261.02

構造登録者

Kong, X.-P.,Kuriyan, J. (登録日: 1992-11-13, 公開日: 1994-01-31, 最終更新日: 2024-02-21)

主引用文献

Kong, X.P.,Onrust, R.,O'Donnell, M.,Kuriyan, J.
Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp.
Cell(Cambridge,Mass.), 69:425-437, 1992

PubMed Abstract: The crystal structure of the beta subunit (processivity factor) of DNA polymerase III holoenzyme has been determined at 2.5 A resolution. A dimer of the beta subunit (M(r) = 2 x 40.6 kd, 2 x 366 amino acid residues) forms a ring-shaped structure lined by 12 alpha helices that can encircle duplex DNA. The structure is highly symmetrical, with each monomer containing three domains of identical topology. The charge distribution and orientation of the helices indicate that the molecule functions by forming a tight clamp that can slide on DNA, as shown biochemically. A potential structural relationship is suggested between the beta subunit and proliferating cell nuclear antigen (PCNA, the eukaryotic polymerase delta [and epsilon] processivity factor), and the gene 45 protein of the bacteriophage T4 DNA polymerase.

PubMed: 1349852
DOI: 10.1016/0092-8674(92)90445-I

実験手法

X-RAY DIFFRACTION (2.5 Å)