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-Structure paper
タイトル | Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. |
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ジャーナル・号・ページ | Nature, Vol. 410, Issue 6826, Page 331-337, Year 2001 |
掲載日 | 2001年3月15日 |
著者 | F A Samatey / K Imada / S Nagashima / F Vonderviszt / T Kumasaka / M Yamamoto / K Namba / |
PubMed 要旨 | The bacterial flagellar filament is a helical propeller constructed from 11 protofilaments of a single protein, flagellin. The filament switches between left- and right-handed supercoiled forms when ...The bacterial flagellar filament is a helical propeller constructed from 11 protofilaments of a single protein, flagellin. The filament switches between left- and right-handed supercoiled forms when bacteria switch their swimming mode between running and tumbling. Supercoiling is produced by two different packing interactions of flagellin called L and R. In switching from L to R, the intersubunit distance ( approximately 52 A) along the protofilament decreases by 0.8 A. Changes in the number of L and R protofilaments govern supercoiling of the filament. Here we report the 2.0 A resolution crystal structure of a Salmonella flagellin fragment of relative molecular mass 41,300. The crystal contains pairs of antiparallel straight protofilaments with the R-type repeat. By simulated extension of the protofilament model, we have identified possible switch regions responsible for the bi-stable mechanical switch that generates the 0.8 A difference in repeat distance. |
リンク | Nature / PubMed:11268201 |
手法 | X線回折 |
解像度 | 2 Å |
構造データ | PDB-1io1: |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | STRUCTURAL PROTEIN / beta-folium / flagellin |