4KBG
almost closed conformation of the helicase core of the RNA helicase Hera
4KBG の概要
エントリーDOI | 10.2210/pdb4kbg/pdb |
関連するPDBエントリー | 3eaq 3ear 3eas 4KBF |
分子名称 | Heat resistant RNA dependent ATPase, SULFATE ION (3 entities 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 | 80576.27 |
構造登録者 | |
主引用文献 | Klostermeier, D. Rearranging RNA structures at 75C? toward the molecular mechanism and physiological function of the thermus thermophilus DEAD-box helicase hera. Biopolymers, 99:1137-1146, 2013 Cited by PubMed Abstract: DEAD-box helicases catalyze the ATP-dependent destabilization of RNA duplexes. Hera is a DEAD-box helicase from Thermus thermophilus that consists of a helicase core, followed by a C-terminal extension comprising a dimerization domain and an RNA-binding domain. The combined structural information on individual Hera domains provides a molecular model of the Hera dimer. The modular architecture with flexible connections between individual domains affords different relative orientations of the RBD relative to the Hera helicase core, and of the two helicase cores within the dimer. Presumably, domain movements are intimately linked to RNA binding, to the interplay of the RBD and the helicase core, and to RNA unwinding, and may impact on the functional cooperation of the two helicase cores in RNA unwinding. The in vivo function of Hera is unknown. The Hera RBD recognizes two distinct elements in the RNA substrate, a single-stranded and a structured region. The helicase core then unwinds an adjacent RNA duplex in an ATP-dependent reaction. Overall, this mode of action is reminiscent of DEAD-box proteins that act as general RNA chaperones. This review summarizes the current knowledge on Hera structure and function, and discusses a possible role of Hera in the Thermus thermophilus cold-shock response. PubMed: 23765433DOI: 10.1002/bip.22316 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.54 Å) |
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