1CR1

CRYSTAL STRUCTURE OF THE HELICASE DOMAIN OF THE GENE 4 PROTEIN OF BACTERIOPHAGE T7: COMPLEX WITH DTTP

1CR1 の概要

• エントリーDOI: 10.2210/pdb1cr1/pdb
• 関連するPDBエントリー: 1CR0 1CR2 1CR4
• 分子名称: DNA PRIMASE/HELICASE, SULFATE ION, THYMIDINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: reca-type fold, transferase
• 由来する生物種: Enterobacteria phage T7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33506.27

構造登録者

Sawaya, M.R.,Guo, S.,Tabor, S.,Richardson, C.C.,Ellenberger, T. (登録日: 1999-08-12, 公開日: 1999-11-10, 最終更新日: 2024-02-07)

主引用文献

Sawaya, M.R.,Guo, S.,Tabor, S.,Richardson, C.C.,Ellenberger, T.
Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7.
Cell(Cambridge,Mass.), 99:167-177, 1999

PubMed Abstract: Helicases that unwind DNA at the replication fork are ring-shaped oligomeric enzymes that move along one strand of a DNA duplex and catalyze the displacement of the complementary strand in a reaction that is coupled to nucleotide hydrolysis. The helicase domain of the replicative helicase-primase protein from bacteriophage T7 crystallized as a helical filament that resembles the Escherichia coli RecA protein, an ATP-dependent DNA strand exchange factor. When viewed in projection along the helical axis of the crystals, six protomers of the T7 helicase domain resemble the hexameric rings seen in electron microscopic images of the intact T7 helicase-primase. Nucleotides bind at the interface between pairs of adjacent subunits where an arginine is near the gamma-phosphate of the nucleotide in trans. The bound nucleotide stabilizes the folded conformation of a DNA-binding motif located near the center of the ring. These and other observations suggest how conformational changes are coupled to DNA unwinding activity.

PubMed: 10535735
DOI: 10.1016/S0092-8674(00)81648-7

実験手法

X-RAY DIFFRACTION (2.3 Å)