1PJR

STRUCTURE OF DNA HELICASE

1PJR の概要

• エントリーDOI: 10.2210/pdb1pjr/pdb
• 分子名称: PCRA (2 entities in total)
• 機能のキーワード: dna repair, dna replication, sos response, helicase, atp-binding, dna-binding
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 82595.10

構造登録者

Subramanya, H.S.,Bird, L.E.,Brannigan, J.A.,Wigley, D.B. (登録日: 1996-10-11, 公開日: 1997-12-03, 最終更新日: 2024-02-14)

主引用文献

Subramanya, H.S.,Bird, L.E.,Brannigan, J.A.,Wigley, D.B.
Crystal structure of a DExx box DNA helicase.
Nature, 384:379-383, 1996

PubMed Abstract: There are a wide variety of helicases that unwind helical DNA and RNA substrates. The twelve helicases that have been identified in Escherichia coli play a role in almost all cellular processes involving nucleic acids. We have solved the crystal structure of a monomeric form of a DNA helicase from Bacillus stearothermophilus, alone and in a complex with ADP, at 2.5 and 2.9 A resolution, respectively. The enzyme comprises two domains with a deep cleft running between them. The ATP-binding site, which is situated at the bottom of this cleft, is formed by motifs that are conserved across the superfamily of related helicases. Unexpected structural homology with the DNA recombination protein, RecA, suggests how ATP binding and hydrolysis may drive conformational changes of the enzyme during catalysis, and implies that there is a common mechanism for all helicases.

PubMed: 8934527
DOI: 10.1038/384379a0

実験手法

X-RAY DIFFRACTION (2.5 Å)