EMD-20504
10 Angstrom structure of the asymmetric flagellar filament purified from Leptospira biflexa Patoc WT cells resolved via subtomogram averaging
EMD-20504
Subtomogram averaging9.83 Å
Deposition: 22/07/2019Map released: 25/03/2020
Last modified: 20/03/2024
Sample Organism:
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
Sample: Flagellar filament purified from the periplasm of the Spirochete bacterium, Leptospira biflexa
Fitted models: 6pwb
Deposition Authors: Gibson KH
,
Sindelar CV
Sample: Flagellar filament purified from the periplasm of the Spirochete bacterium, Leptospira biflexa
Fitted models: 6pwb
Deposition Authors: Gibson KH
,
Sindelar CV
An asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete.
Gibson KH ,
Trajtenberg F ,
Wunder EA ,
Brady MR,
San Martin F ,
Mechaly A ,
Shang Z,
Liu J,
Picardeau M,
Ko A ,
Buschiazzo A ,
Sindelar CV
(2020) eLife , 9
,
Trajtenberg F ,
Wunder EA ,
Brady MR,
San Martin F ,
Mechaly A ,
Shang Z,
Liu J,
Picardeau M,
Ko A ,
Buschiazzo A ,
Sindelar CV
(2020) eLife , 9
Secondary citations:
- San Martin F, Mechaly AE, Larrieux N, Wunder EA, Ko AI, Picardeau M, Trajtenberg F & Buschiazzo A. (2017) Crystallization of FcpA from Leptospira, a novel flagellar protein that is essential for pathogenesis. Acta Crystallogr F Struct Biol Commun, 73, 123 - 129
- Wunder EA, Figueira CP, Benaroudj N, Hu B, Tong BA, Trajtenberg F, Liu J, Reis MG, Charon NW, Buschiazzo A, Picardeau M & Ko AI. (2016) A novel flagellar sheath protein, FcpA, determines filament coiling, translational motility and virulence for the Leptospira spirochete. Mol Microbiol, 101, 457 - 470
- Wunder EA, Slamti L, Suwondo DN, Gibson KH, Shang Z, Sindelar CV, Trajtenberg F, Buschiazzo A, Ko AI & Picardeau M. (2018) FcpB Is a Surface Filament Protein of the Endoflagellum Required for the Motility of the Spirochete. Front Cell Infect Microbiol, 8, 130