Proteopedia:Featured JRN/1

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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>
<tr><td><div class="scrolling">'''Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in ''Salmonella enterica''.'''<br>
''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>
''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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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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