User:Fadel A. Samatey/FlhBc I
From Proteopedia
(→Molecular Tour: FlhBc Structures) |
(→Molecular Tour: FlhBc Structures) |
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====''Aquifex''==== | ====''Aquifex''==== | ||
| - | FlhB from the thermophile<ref>[http://en.wikipedia.org/wiki/Aquifex_aeolicus Optimum growth ~90<sup>o</sup> C].</ref> ''Aquifex aeolicus'' is shorter, 350 residues (vs. 383 for ''S. typhimurium''), with 32% sequence identity. Residues 213-350 (length 138) were crystallized, and the resulting model [[3b1s]] has <scene name='User:Fadel_A._Samatey/FlhBc_I/Triple-au-aquifex/1'>three molecules</scene> in the [[asymmetric unit]]. The molecule displayed | + | FlhB from the thermophile<ref>[http://en.wikipedia.org/wiki/Aquifex_aeolicus Optimum growth ~90<sup>o</sup> C].</ref> ''Aquifex aeolicus'' is shorter, 350 residues (vs. 383 for ''S. typhimurium''), with 32% sequence identity. Residues 213-350 (length 138) were crystallized, and the resulting model [[3b1s]] has <scene name='User:Fadel_A._Samatey/FlhBc_I/Triple-au-aquifex/1'>three molecules</scene> in the [[asymmetric unit]]. The molecule displayed in the comparison in the next section, with chains designated C and D, was chosen because it has the lowest average [[temperature factor]] (66.2, vs. 84.7 and 72.6 for A,B and E,F respectively). It has coordinates for 232-337 (length 106, 77% of the crystallized segment), cleaved at NPTH between Asn263 and Pro264. |
====Comparison==== | ====Comparison==== | ||
Revision as of 12:28, 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
