6pwb | pdb_00006pwb

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

spinqualitylabelsall models 6pwb, resolution 9.83Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6pwb is a 163 chain structure with sequence from Leptospira biflexa serovar patoc (strain patoc 1 / atcc 23582 / paris). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 5wjt, 6nqz, 6nqw, 6nqx, 6nqy Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [B0SSZ5_LEPBP] Component of the core of the flagella.[RuleBase:RU362073] Publication Abstract from PubMed 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 Leptospira 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. 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 Elife. 2020 Mar 11;9. pii: 53672. doi: 10.7554/eLife.53672. PMID:32157997 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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