6ZWW

Crystal structure of E. coli RNA helicase HrpA in complex with RNA

6ZWW の概要

• エントリーDOI: 10.2210/pdb6zww/pdb
• 分子名称: ATP-dependent RNA helicase HrpA, ssRNA, CALCIUM ION (3 entities in total)
• 機能のキーワード: rna helicase, ntpase, bacterial helicase, dexh-box, rna binding protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 373106.35

構造登録者

Grass, L.M.,Wollenhaupt, J.,Barthel, T.,Loll, B.,Wahl, M.C. (登録日: 2020-07-29, 公開日: 2021-06-30, 最終更新日: 2024-01-31)

主引用文献

Grass, L.M.,Wollenhaupt, J.,Barthel, T.,Parfentev, I.,Urlaub, H.,Loll, B.,Klauck, E.,Antelmann, H.,Wahl, M.C.
Large-scale ratcheting in a bacterial DEAH/RHA-type RNA helicase that modulates antibiotics susceptibility.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: Many bacteria harbor RNA-dependent nucleoside-triphosphatases of the DEAH/RHA family, whose molecular mechanisms and cellular functions are poorly understood. Here, we show that the DEAH/RHA protein, HrpA, is an ATP-dependent 3 to 5' RNA helicase and that the RNA helicase activity of HrpA influences bacterial survival under antibiotics treatment. Limited proteolysis, crystal structure analysis, and functional assays showed that HrpA contains an N-terminal DEAH/RHA helicase cassette preceded by a unique N-terminal domain and followed by a large C-terminal region that modulates the helicase activity. Structures of an expanded HrpA helicase cassette in the apo and RNA-bound states in combination with cross-linking/mass spectrometry revealed ratchet-like domain movements upon RNA engagement, much more pronounced than hitherto observed in related eukaryotic DEAH/RHA enzymes. Structure-based functional analyses delineated transient interdomain contact sites that support substrate loading and unwinding, suggesting that similar conformational changes support RNA translocation. Consistently, modeling studies showed that analogous dynamic intramolecular contacts are not possible in the related but helicase-inactive RNA-dependent nucleoside-triphosphatase, HrpB. Our results indicate that HrpA may be an interesting target to interfere with bacterial tolerance toward certain antibiotics and suggest possible interfering strategies.

PubMed: 34290142
DOI: 10.1073/pnas.2100370118

実験手法

X-RAY DIFFRACTION (3.16 Å)