1DML

CRYSTAL STRUCTURE OF HERPES SIMPLEX UL42 BOUND TO THE C-TERMINUS OF HSV POL

1DML の概要

• エントリーDOI: 10.2210/pdb1dml/pdb
• 関連するPDBエントリー: 1axc 1b8h 1plq
• 分子名称: DNA POLYMERASE PROCESSIVITY FACTOR, DNA POLYMERASE (2 entities in total)
• 機能のキーワード: herpes simplex virus, dna synthesis, sliding clamps, pcna, processivity, dna binding protein-transferase complex, dna binding protein/transferase
• 由来する生物種: Human herpesvirus 1 (Herpes simplex virus type 1); 詳細
• 細胞内の位置: Host nucleus: P10226 P07917
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 151932.30

構造登録者

Zuccola, H.J.,Filman, D.J.,Coen, D.M.,Hogle, J.M. (登録日: 1999-12-14, 公開日: 2000-03-15, 最終更新日: 2024-02-07)

主引用文献

Zuccola, H.J.,Filman, D.J.,Coen, D.M.,Hogle, J.M.
The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase.
Mol.Cell, 5:267-278, 2000

PubMed Abstract: Herpes simplex virus DNA polymerase is a heterodimer composed of a catalytic subunit, Pol, and an unusual processivity subunit, UL42, which, unlike processivity factors such as PCNA, directly binds DNA. The crystal structure of a complex of the C-terminal 36 residues of Pol bound to residues 1-319 of UL42 reveals remarkable similarities between UL42 and PCNA despite contrasting biochemical properties and lack of sequence homology. Moreover, the Pol-UL42 interaction resembles the interaction between the cell cycle regulator p21 and PCNA. The structure and previous data suggest that the UL42 monomer interacts with DNA quite differently than does multimeric toroidal PCNA. The details of the structure lead to a model for the mechanism of UL42, provide the basis for drug design, and allow modeling of other proteins that lack sequence homology with UL42 or PCNA.

PubMed: 10882068
DOI: 10.1016/S1097-2765(00)80422-0

実験手法

X-RAY DIFFRACTION (2.7 Å)