6EUD

Crystal structure of E. coli DExH-box NTPase HrpB

6EUD の概要

• エントリーDOI: 10.2210/pdb6eud/pdb
• 分子名称: ATP-dependent RNA helicase HrpB, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: hrpb, deah/rha helicase, bacterial helicase, rna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 89645.18

構造登録者

Pietrzyk-Brzezinska, A.J.,Wahl, M.C. (登録日: 2017-10-30, 公開日: 2018-09-12, 最終更新日: 2024-05-08)

主引用文献

Pietrzyk-Brzezinska, A.J.,Absmeier, E.,Klauck, E.,Wen, Y.,Antelmann, H.,Wahl, M.C.
Crystal Structure of the Escherichia coli DExH-Box NTPase HrpB.
Structure, 26:1462-1473.e4, 2018

PubMed Abstract: Eukaryotic DExH-box proteins are important post-transcriptional gene regulators, many of which employ RNA-stimulated nucleoside triphosphatase activity to remodel RNAs or ribonucleoprotein complexes. However, bacterial DExH-box proteins are structurally and functionally poorly characterized. We report the crystal structure of the Escherichia coli DExH-box protein HrpB. A globular head is composed of dual RecA, winged-helix, helical bundle and oligonucleotide/oligosaccharide-binding domains, resembling a compact version of eukaryotic DExH-box proteins. Additionally, HrpB harbors a C-terminal region not found in proteins with known structure, which bestows the protein with unique interaction potential. Interaction and activity assays showed that the protein binds RNA but not DNA, hydrolyzes all nucleoside triphosphates in an RNA-stimulated manner, but does not unwind diverse model RNAs in vitro. These observations can be rationalized by detailed comparisons with structurally characterized eukaryotic DExH-box proteins. Comparative phenotypic analyses of an E. coli hrpB knockout mutant suggested diverse functions of HrpB homologs in different bacteria.

PubMed: 30174149
DOI: 10.1016/j.str.2018.07.013

実験手法

X-RAY DIFFRACTION (2.4 Å)