Proteopedia:Featured JRN/1

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<tr><td>[[Image:Anim Samatey2 FigA I.gif]]</td></tr>
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<tr><td>'''Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica.'''</td></tr>
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<tr><td>''Hideyuki Matsunami, Young-Ho Yoon, Vladimir Meshcheryakov, Keiichi Namba, and Fadel A. Samatey''<br>Scientific Reports 6:27399 2016 doi: [http://dx.doi.org/10.1038/srep27399 10.1038/srep27399]</td></tr>
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<tr><td>A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. The mechanism of chaperone-mediated P-ring formation is poorly understood. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.</td></tr>
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default [[User:Fadel_A._Samatey/FlgA_I]]
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<tr><td><div class="scrolling">'''Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in ''Salmonella enterica''.'''<br>
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''H Matsunami, YH Yoon, VA Meshcheryakov, K Namba, FA Samatey''. Scientific Reports 2016 doi: [http://dx.doi.org/10.1038/srep27399 10.1038/srep27399]<br>
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A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as ''Salmonella enterica'' or ''Escherichia coli''. Here we present the open and closed crystal structures of FlgA from ''Salmonella enterica serovar Typhimurium'', grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.
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>>> [[User:Fadel_A._Samatey/FlgA_I|Visit this I3DC complement]] >>>
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[[Category:Featured in I3DC]]

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Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica.

H Matsunami, YH Yoon, VA Meshcheryakov, K Namba, FA Samatey. Scientific Reports 2016 doi: 10.1038/srep27399
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.

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