2GXU

HERA N-terminal domain in complex with orthophosphate, crystal form 1

2GXU の概要

• エントリーDOI: 10.2210/pdb2gxu/pdb
• 関連するPDBエントリー: 2GXQ 2GXS
• 分子名称: heat resistant RNA dependent ATPase, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: rna helicase, atomic resolution, amp complex, ribosome biogenesis, thermophilic, hydrolase
• 由来する生物種: Thermus thermophilus HB27
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22437.92

構造登録者

Rudolph, M.G.,Klostermeier, D. (登録日: 2006-05-09, 公開日: 2006-08-22, 最終更新日: 2024-02-14)

主引用文献

Rudolph, M.G.,Heissmann, R.,Wittmann, J.G.,Klostermeier, D.
Crystal Structure and Nucleotide Binding of the Thermus thermophilus RNA Helicase Hera N-terminal Domain.
J.Mol.Biol., 351:731-743, 2006

PubMed Abstract: DEAD box RNA helicases use the energy of ATP hydrolysis to unwind double-stranded RNA regions or to disrupt RNA/protein complexes. A minimal RNA helicase comprises nine conserved motifs distributed over two RecA-like domains. The N-terminal domain contains all motifs involved in nucleotide binding, namely the Q-motif, the DEAD box, and the P-loop, as well as the SAT motif, which has been implicated in the coordination of ATP hydrolysis and RNA unwinding. We present here the crystal structure of the N-terminal domain of the Thermus thermophilus RNA helicase Hera in complex with adenosine monophosphate (AMP). Upon binding of AMP the P-loop adopts a partially collapsed or half-open conformation that is still connected to the DEAD box motif, and the DEAD box in turn is linked to the SAT motif via hydrogen bonds. This network of interactions communicates changes in the P-loop conformation to distant parts of the helicase. The affinity of AMP is comparable to that of ADP and ATP, substantiating that the binding energy from additional phosphate moieties is directly converted into conformational changes of the entire helicase. Importantly, the N-terminal Hera domain forms a dimer in the crystal similar to that seen in another thermophilic prokaryote. It is possible that this mode of dimerization represents the prototypic architecture in RNA helicases of thermophilic origin.

PubMed: 16890241
DOI: 10.1016/j.jmb.2006.06.065

実験手法

X-RAY DIFFRACTION (1.67 Å)