6PWB

Rigid body fitting of flagellin FlaB, and flagellar coiling proteins, FcpA and FcpB, into a 10 Angstrom structure of the asymmetric flagellar filament purified from Leptospira biflexa Patoc WT cells resolved via subtomogram averaging

これはPDB形式変換不可エントリーです。

6PWB の概要

• エントリーDOI: 10.2210/pdb6pwb/pdb
• 関連するPDBエントリー: 5WJT 6NQW 6NQX 6NQY 6NQZ
• EMDBエントリー: 20504
• 分子名称: Flagellin B1 (FlaB1), Flagellar coiling protein A (FcpA), Flagellar coiling protein B (FcpB) (3 entities in total)
• 機能のキーワード: bacterial flagella, fcpa, fcpb, flaa, flab, leptospira, structural protein
• 由来する生物種: Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris); 詳細
• タンパク質・核酸の鎖数: 163
• 化学式量合計: 4652257.18

構造登録者

Gibson, K.H.,Sindelar, C.V.,Trajtenberg, F.,Buschiazzo, A.,San Martin, F.,Mechaly, A. (登録日: 2019-07-22, 公開日: 2020-03-25, 最終更新日: 2024-03-20)

主引用文献

Gibson, K.H.,Trajtenberg, F.,Wunder, E.A.,Brady, M.R.,San Martin, F.,Mechaly, A.,Shang, Z.,Liu, J.,Picardeau, M.,Ko, A.,Buschiazzo, A.,Sindelar, C.V.
An asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete.
Elife, 9:-, 2020

PubMed Abstract: Spirochete bacteria, including important pathogens, exhibit a distinctive means of swimming via undulations of the entire cell. Motility is powered by the rotation of supercoiled 'endoflagella' that wrap around the cell body, confined within the periplasmic space. To investigate the structural basis of flagellar supercoiling, which is critical for motility, we determined the structure of native flagellar filaments from the spirochete by integrating high-resolution cryo-electron tomography and X-ray crystallography. We show that these filaments are coated by a highly asymmetric, multi-component sheath layer, contrasting with flagellin-only homopolymers previously observed in exoflagellated bacteria. Distinct sheath proteins localize to the filament inner and outer curvatures to define the supercoiling geometry, explaining a key functional attribute of this spirochete flagellum.

PubMed: 32157997
DOI: 10.7554/eLife.53672

実験手法

ELECTRON MICROSCOPY (9.83 Å)