User:Fadel A. Samatey/FlhBc I
From Proteopedia
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===Brief Introduction=== | ===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 | + | 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 [http://dx.doi.org/10.1107/S0907444913002102 the publication] for a more detailed introduction.) | (Please see [http://dx.doi.org/10.1107/S0907444913002102 the publication] for a more detailed introduction.) | ||
Revision as of 12:12, 29 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. 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
Notes for Developers
- Image:Workbench 3b0z.pdb.gz
- Image:Workbench 3b1s.pdb.gz
- Image:Workbench 3b0z 3b1sCD.pdb 1.1 is 3b0z(St) while 1.2 is 3b1s chains C and D. Not aligned.
- Image:Workbench 3b0z 3b1sCD aligned.pdb
