5FHF

Crystal structure of Bacteroides sp Pif1 in complex with ADP-AlF4

5FHF の概要

• エントリーDOI: 10.2210/pdb5fhf/pdb
• 関連するPDBエントリー: 5FHD 5FHE 5FHG 5FHH
• 分子名称: Uncharacterized protein, ADENOSINE-5'-DIPHOSPHATE, TETRAFLUOROALUMINATE ION, ... (4 entities in total)
• 機能のキーワード: pif1 helicase, dna helicase, hydrolase
• 由来する生物種: Bacteroides sp. 2_1_16
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50247.12

構造登録者

Zhou, X.,Ren, W.,Bharath, S.R.,Song, H. (登録日: 2015-12-22, 公開日: 2016-03-30, 最終更新日: 2024-03-20)

主引用文献

Zhou, X.,Ren, W.,Bharath, S.R.,Tang, X.,He, Y.,Chen, C.,Liu, Z.,Li, D.,Song, H.
Structural and Functional Insights into the Unwinding Mechanism of Bacteroides sp Pif1
Cell Rep, 14:2030-2039, 2016

PubMed Abstract: Pif1 is a conserved SF1B DNA helicase involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. Here, we report the structures of the helicase domain of human Pif1 and Bacteroides sp Pif1 (BaPif1) in complex with ADP-AlF4(-) and two different single-stranded DNAs (ssDNAs). The wedge region equivalent to the β hairpin in other SF1B DNA helicases folds into an extended loop followed by an α helix. The Pif1 signature motif of BaPif1 interacts with the wedge region and a short helix in order to stabilize these ssDNA binding elements, therefore indirectly exerting its functional role. Domain 2B of BaPif1 undergoes a large conformational change upon concomitant binding of ATP and ssDNA, which is critical for Pif1's activities. BaPif1 cocrystallized with a tailed dsDNA and ADP-AlF4(-), resulting in a bound ssDNA bent nearly 90° at the ssDNA/dsDNA junction. The conformational snapshots of BaPif1 provide insights into the mechanism governing the helicase activity of Pif1.

PubMed: 26904952
DOI: 10.1016/j.celrep.2016.02.008

実験手法

X-RAY DIFFRACTION (2.15 Å)