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Science 15 December 2000:
Vol. 290. no. 5499, pp. 2148 - 2152
DOI: 10.1126/science.290.5499.2148
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Reports

The Bacterial Flagellar Cap as the Rotary Promoter of Flagellin Self-Assembly

Koji Yonekura,1* Saori Maki,1* David Gene Morgan,2 David J. DeRosier,3 Ferenc Vonderviszt,4 Katsumi Imada,1 Keiichi Namba15dagger

The growth of the bacterial flagellar filament occurs at its distal end by self-assembly of flagellin transported from the cytoplasm through the narrow central channel. The cap at the growing end is essential for its growth, remaining stably attached while permitting the flagellin insertion. In order to understand the assembly mechanism, we used electron microscopy to study the structures of the cap-filament complex and isolated cap dimer. Five leg-like anchor domains of the pentameric cap flexibly adjusted their conformations to keep just one flagellin binding site open, indicating a cap rotation mechanism to promote the flagellin self-assembly. This represents one of the most dynamic movements in protein structures.

1 Protonic NanoMachine Project, ERATO, JST, 3-4 Hikaridai, Seika, Kyoto 619-0237, Japan.
2 Department of Biophysics, Boston University School of Medicine, Boston, MA 02118, and Department of Cell Biology, Harvard Medical School, Boston, MA 02254, USA.
3 Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254, USA.
4 Department of Physics, University of Veszprém, Egyetem Street 10, H-8201 Veszprém, Hungary.
5 Advanced Technology Research Laboratories, Matsushita Electric Industrial Co., Ltd., 3-4 Hikaridai, Seika, Kyoto 619-0237 Japan.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed. E-mail: keiichi{at}crl.mei.co.jp

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