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

This is a non-PDB format compatible entry.

Summary for 6PWB

• Entry DOI: 10.2210/pdb6pwb/pdb
• Related: 5WJT 6NQW 6NQX 6NQY 6NQZ
• EMDB information: 20504
• Descriptor: Flagellin B1 (FlaB1), Flagellar coiling protein A (FcpA), Flagellar coiling protein B (FcpB) (3 entities in total)
• Functional Keywords: bacterial flagella, fcpa, fcpb, flaa, flab, leptospira, structural protein
• Biological source: Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris); More
• Total number of polymer chains: 163
• Total formula weight: 4652257.18

Authors

Gibson, K.H.,Sindelar, C.V.,Trajtenberg, F.,Buschiazzo, A.,San Martin, F.,Mechaly, A. (deposition date: 2019-07-22, release date: 2020-03-25, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (9.83 Å)