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-Structure paper
タイトル | An asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete. |
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ジャーナル・号・ページ | Elife, Vol. 9, Year 2020 |
掲載日 | 2020年3月11日 |
著者 | Kimberley H Gibson / Felipe Trajtenberg / Elsio A Wunder / Megan R Brady / Fabiana San Martin / Ariel Mechaly / Zhiguo Shang / Jun Liu / Mathieu Picardeau / Albert Ko / Alejandro Buschiazzo / Charles Vaughn Sindelar / |
PubMed 要旨 | 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 ...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. |
リンク | Elife / PubMed:32157997 / PubMed Central |
手法 | EM (サブトモグラム平均) |
解像度 | 9.83 - 18.4 Å |
構造データ | EMDB-20503: EMDB-20504: 10 Angstrom structure of the asymmetric flagellar filament purified from Leptospira biflexa Patoc WT cells resolved via subtomogram averaging |
由来 |
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キーワード | STRUCTURAL PROTEIN / bacterial flagella / FcpA / FcpB / FlaA / FlaB / Leptospira |