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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 Namba15
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.
To whom correspondence should be addressed. E-mail:
keiichi{at}crl.mei.co.jp
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