5TNU

S. tokodaii XPB II crystal structure at 3.0 Angstrom resolution

5TNU の概要

• エントリーDOI: 10.2210/pdb5tnu/pdb
• 分子名称: DNA-dependent ATPase XPBII, SULFATE ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: helicase, ner, transcription
• 由来する生物種: Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 107820.04

構造登録者

DuPrez, K.T.,Hilario, E.,Wang, I.,Fan, L. (登録日: 2016-10-14, 公開日: 2017-11-01, 最終更新日: 2023-10-04)

主引用文献

Kahanda, D.,DuPrez, K.T.,Hilario, E.,McWilliams, M.A.,Wohlgamuth, C.H.,Fan, L.,Slinker, J.D.
Application of Electrochemical Devices to Characterize the Dynamic Actions of Helicases on DNA.
Anal.Chem., 90:2178-2185, 2018

PubMed Abstract: Much remains to be understood about the kinetics and thermodynamics of DNA helicase binding and activity. Here, we utilize probe-modified DNA monolayers on multiplexed gold electrodes as a sensitive recognition element and morphologically responsive transducer of helicase-DNA interactions. The electrochemical signals from these devices are highly sensitive to structural distortion of the DNA produced by the helicases. We used this DNA electrochemistry to distinguish the details of the DNA interactions of three distinct XPB helicases, which belong to the superfamily-2 of helicases. Clear changes in DNA melting temperature and duplex stability were observed upon helicase binding, shifts that could not be observed with conventional UV-visible absorption measurements. Binding dissociation constants were estimated in the range from 10 to 50 nM and correlated with observations of activity. ATP-stimulated DNA unwinding activity was also followed, revealing exponential time scales and distinct time constants associated with conventional and molecular wrench modes of operation further confirmed by crystal structures. These devices thus provide a sensitive measure of the structural thermodynamics and kinetics of helicase-DNA interactions.

PubMed: 29285929
DOI: 10.1021/acs.analchem.7b04515

実験手法

X-RAY DIFFRACTION (3.05 Å)