3EAS

Novel dimerization motif in the DEAD box RNA helicase Hera: form 1, complete dimer, asymmetric

3EAS の概要

• エントリーDOI: 10.2210/pdb3eas/pdb
• 関連するPDBエントリー: 3eaq 3ear
• 分子名称: Hera (1 entity in total)
• 機能のキーワード: dead box rna helicase, dimer, atp-binding, helicase, hydrolase, nucleotide-binding
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47734.55

構造登録者

Klostermeier, D.,Rudolph, M.G. (登録日: 2008-08-26, 公開日: 2008-12-09, 最終更新日: 2023-08-30)

主引用文献

Klostermeier, D.,Rudolph, M.G.
A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility.
Nucleic Acids Res., 37:421-430, 2009

PubMed Abstract: DEAD box helicases are involved in nearly all aspects of RNA metabolism. They share a common helicase core, and may comprise additional domains that contribute to RNA binding. The Thermus thermophilus helicase Hera is the first dimeric DEAD box helicase. Crystal structures of Hera fragments reveal a bipartite C-terminal domain with a novel dimerization motif and an RNA-binding module. We provide a first glimpse on the additional RNA-binding module outside the Hera helicase core. The dimerization and RNA-binding domains are connected to the C-terminal RecA domain by a hinge region that confers exceptional flexibility onto the helicase, allowing for different juxtapositions of the RecA-domains in the dimer. Combination of the previously determined N-terminal Hera structure with the C-terminal Hera structures allows generation of a model for the entire Hera dimer, where two helicase cores can work in conjunction on large RNA substrates.

PubMed: 19050012
DOI: 10.1093/nar/gkn947

実験手法

X-RAY DIFFRACTION (2.8 Å)