User:Fadel A. Samatey/FlhBc I
From Proteopedia
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===Flexibility of N-Terminus=== | ===Flexibility of N-Terminus=== | ||
Molecular dynamics simulations suggested that the mutations in 281-285 reduced flexibility of the N-terminal alpha helix, and hence that such flexibility may be important for function. Indeed, 226-267 (the N-terminal helix is 229 to about 262) is predicted to be intrinsically disordered<ref>Prediction of intrinsic disorder for ''Salmonella typhimurium'' FlhB by the FoldIndex server (image below, at right). [[Image:3b0z-FlhB-foldindex.png|frame]]</ref>. The formation of a helix seems likely to be the result of stabilization by crystal contacts mentioned above. | Molecular dynamics simulations suggested that the mutations in 281-285 reduced flexibility of the N-terminal alpha helix, and hence that such flexibility may be important for function. Indeed, 226-267 (the N-terminal helix is 229 to about 262) is predicted to be intrinsically disordered<ref>Prediction of intrinsic disorder for ''Salmonella typhimurium'' FlhB by the FoldIndex server (image below, at right). [[Image:3b0z-FlhB-foldindex.png|frame]]</ref>. The formation of a helix seems likely to be the result of stabilization by crystal contacts mentioned above. | ||
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| + | ===Evolutionary Conservation=== | ||
| + | <scene name='User:Fadel_A._Samatey/FlhBc_I/Conservation_st/1'>Conservation of FlhBc (''S. typhimurium'')</scene> was calculated by the [http://consurf.tau.ac.il ConSurf Server]. | ||
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</StructureSection> | </StructureSection> | ||
===References and Notes=== | ===References and Notes=== | ||
Revision as of 10:29, 30 April 2013
Interactive 3D Complement in Proteopedia
Inhibition of a type III secretion system by the deletion of a short loop in one of its membrane proteins.
Vladimir A. Meshcheryakov, Akio Kitao, Hideyuki Matsunami and Fadel A. Samatey (サマテ). Acta Cryst. D69: 812-820 (2013). doi:10.1107/S0907444913002102
Brief Introduction
FlhB is a membrane protein that is part of the flagellum-specific secretion apparatus. It is required for secretion of flagellar proteins, and for bacterial motility. FlhB is paralogous to a protein in the virulence type III secretion system. FlhB has a hydrophobic integral membrane domain, predicted to have four transmembrane helices, a flexible linker that is highly conserved and essential for function, and a cytoplasmic domain. The present study reports the structures of the cytoplasmic domains of two bacterial taxa. (Please see the publication for a more detailed introduction.)
Molecular Tour: FlhBc Structures
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References and Notes
- ↑ Optimum growth ~90o C.
- ↑ Prediction of intrinsic disorder for Salmonella typhimurium FlhB by the FoldIndex server (image below, at right).
