F
Ferenc Vonderviszt
Researcher at University of Pannonia
Publications - 87
Citations - 2861
Ferenc Vonderviszt is an academic researcher from University of Pannonia. The author has contributed to research in topics: Flagellin & Protein filament. The author has an hindex of 27, co-authored 81 publications receiving 2708 citations. Previous affiliations of Ferenc Vonderviszt include Nagoya University & Hungarian Academy of Sciences.
Papers
More filters
Journal ArticleDOI
Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling.
Fadel A. Samatey,Katsumi Imada,Shigehiro Nagashima,Ferenc Vonderviszt,Takashi Kumasaka,Masaki Yamamoto,Keiichi Namba +6 more
TL;DR: By simulated extension of the protofilament model, it is identified possible switch regions responsible for the bi-stable mechanical switch that generates the 0.8 Å difference in repeat distance.
Journal ArticleDOI
The bacterial flagellar cap as the rotary promoter of flagellin self-assembly
Koji Yonekura,S. Maki,David Gene Morgan,David J. DeRosier,Ferenc Vonderviszt,Katsumi Imada,Keiichi Namba +6 more
Abstract: 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.
Journal ArticleDOI
Structure of the core and central channel of bacterial flagella
TL;DR: X-ray fibre diffraction analysis of bacterial flagellar filaments has allowed the subunit packing and secondary structure arrangement in the filament core to be determined.
Journal ArticleDOI
Molecular architecture of bacterial flagellum
Keiichi Namba,Ferenc Vonderviszt +1 more
Journal ArticleDOI
Terminal regions of flagellin are disordered in solution
TL;DR: Analysis of the calorimetric melting profiles suggests that terminal parts of flagellin have no significant internal stability and they are in extensive contact with water, but these regions contain some secondary structure, probably alpha-helices, as revealed by comparison of the circular dichroic spectra in the far-ultraviolet region.