4WIA

Crystal structure of flagellar accessory protein FlaH from Methanocaldococcus jannaschii

4WIA の概要

• エントリーDOI: 10.2210/pdb4wia/pdb
• 分子名称: Putative flagella-related protein H, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: archaea, flagella, atp-binding protein
• 由来する生物種: Methanocaldococcus jannaschii DSM 2661
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 80447.42

構造登録者

Meshcheryakov, V.A.,Wolf, M. (登録日: 2014-09-25, 公開日: 2015-10-07, 最終更新日: 2024-10-30)

主引用文献

Meshcheryakov, V.A.,Wolf, M.
Crystal structure of the flagellar accessory protein FlaH of Methanocaldococcus jannaschii suggests a regulatory role in archaeal flagellum assembly.
Protein Sci., 25:1147-1155, 2016

PubMed Abstract: Archaeal flagella are unique structures that share functional similarity with bacterial flagella, but are structurally related to bacterial type IV pili. The flagellar accessory protein FlaH is one of the conserved components of the archaeal motility system. However, its function is not clearly understood. Here, we present the 2.2 Å resolution crystal structure of FlaH from the hyperthermophilic archaeon, Methanocaldococcus jannaschii. The protein has a characteristic RecA-like fold, which has been found previously both in archaea and bacteria. We show that FlaH binds to immobilized ATP-however, it lacks ATPase activity. Surface plasmon resonance analysis demonstrates that ATP affects the interaction between FlaH and the archaeal motor protein FlaI. In the presence of ATP, the FlaH-FlaI interaction becomes significantly weaker. A database search revealed similarity between FlaH and several DNA-binding proteins of the RecA superfamily. The closest structural homologs of FlaH are KaiC-like proteins, which are archaeal homologs of the circadian clock protein KaiC from cyanobacteria. We propose that one of the functions of FlaH may be the regulation of archaeal motor complex assembly.

PubMed: 27060465
DOI: 10.1002/pro.2932

実験手法

X-RAY DIFFRACTION (2.2 Å)