User:Fadel A. Samatey/FlgA I

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Scientific Reports an online, open access journal: nature.com/srep


Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica.
Hideyuki Matsunami, Young-Ho Yoon, Vladimir Meshcheryakov, Keiichi Namba, and Fadel A. Samatey.
Scientific Reports 6:27399, June 7, 2016: nature.com/articles/srep27399. (DOI: 10.1038/srep27399)

Notes and References

  1. Matsunami H, Yoon YH, Meshcheryakov VA, Namba K, Samatey FA. Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica. Sci Rep. 2016 Jun 7;6:27399. doi: 10.1038/srep27399. PMID:27273476 doi:http://dx.doi.org/10.1038/srep27399
  2. Residues 1-198 from the open form 3tee were morphed to residues 1-198 of chain A (lowest average temperature) of the closed form 3vki. Residues 44-47 were deleted from the closed form since they were missing in the open form due to disorder. The two chains were globally structurally aligned using the "magic fit" (sequence-based structural alignment) tool in Deepview. A 24-frame linear interpolation morph was performed by the morph server kindly provided by User:Karsten Theis.
  3. In the closed form, the carboxy terminal alpha carbon is 15 Å from D1 (Met43), while in the open form, that distance is 46 Å.
  4. Ohnishi K, Ohto Y, Aizawa S, Macnab RM, Iino T. FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium. J Bacteriol. 1994 Apr;176(8):2272-81. PMID:8157595

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