5YA6

Crystal structure of archaeal flagellin FlaB1 from Methanocaldococcus jannaschii

5YA6 の概要

• エントリーDOI: 10.2210/pdb5ya6/pdb
• 関連するPDBエントリー: 5Z1L
• EMDBエントリー: 6876
• 分子名称: Flagellin B1, CALCIUM ION (3 entities in total)
• 機能のキーワード: archaea, flagellum, flagellin, structural protein
• 由来する生物種: Methanocaldococcus jannaschii DSM 2661
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36971.23

構造登録者

Meshcheryakov, V.A.,Wolf, M. (登録日: 2017-08-30, 公開日: 2019-02-06, 最終更新日: 2024-03-27)

主引用文献

Meshcheryakov, V.A.,Shibata, S.,Schreiber, M.T.,Villar-Briones, A.,Jarrell, K.F.,Aizawa, S.I.,Wolf, M.
High-resolution archaellum structure reveals a conserved metal-binding site.
Embo Rep., 20:-, 2019

PubMed Abstract: Many archaea swim by means of archaella. While the archaellum is similar in function to its bacterial counterpart, its structure, composition, and evolution are fundamentally different. Archaella are related to archaeal and bacterial type IV pili. Despite recent advances, our understanding of molecular processes governing archaellum assembly and stability is still incomplete. Here, we determine the structures of archaella by X-ray crystallography and cryo-EM The crystal structure of FlaB1 is the first and only crystal structure of any archaellin to date at a resolution of 1.5 Å, which is put into biological context by a cryo-EM reconstruction from archaella at 4 Å resolution created with helical single-particle analysis. Our results indicate that the archaellum is predominantly composed of FlaB1. We identify N-linked glycosylation by cryo-EM and mass spectrometry. The crystal structure reveals a highly conserved metal-binding site, which is validated by mass spectrometry and electron energy-loss spectroscopy. We show that the metal-binding site, which appears to be a widespread property of archaellin, is required for filament integrity.

PubMed: 30898768
DOI: 10.15252/embr.201846340

実験手法

X-RAY DIFFRACTION (1.5 Å)