User:Fadel A. Samatey/FlhBc I
From Proteopedia
(→Molecular Tour: FlhBc Structures) |
(→Molecular Tour: FlhBc Structures) |
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==Molecular Tour: FlhBc Structures== | ==Molecular Tour: FlhBc Structures== | ||
<StructureSection size='450' frame='true' align='right' caption='Cytoplasmic domain of FlhB' scene='User:Fadel_A._Samatey/Workbench/I3DC-1/Flhb_st/6' > | <StructureSection size='450' frame='true' align='right' caption='Cytoplasmic domain of FlhB' scene='User:Fadel_A._Samatey/Workbench/I3DC-1/Flhb_st/6' > | ||
| + | <table cellpadding="6" style="background-color:#ffff80"><tr><td> | ||
| + | This page is under construction. We expect to complete additional interactive molecular scenes before May 5, 2013. | ||
| + | </td></tr></table> | ||
====''Salmonella''==== | ====''Salmonella''==== | ||
FlhB from ''Salmonella typhimurium'' consists of 383 amino acids. The cytoplasmic domain 219-383 (length 165, 43% of full length) was crystallized. The resulting model [[3b0z]] includes coordinates for residues 229-353 (length 125, 76% of the crystallized length). The [[asymmetric unit]] contains a single molecule (<scene name='User:Fadel_A._Samatey/Workbench/I3DC-1/Flhb_st/6'>restore initial scene</scene>). As explained in the publication, the position of the long alpha helix appears to be stabilized by | FlhB from ''Salmonella typhimurium'' consists of 383 amino acids. The cytoplasmic domain 219-383 (length 165, 43% of full length) was crystallized. The resulting model [[3b0z]] includes coordinates for residues 229-353 (length 125, 76% of the crystallized length). The [[asymmetric unit]] contains a single molecule (<scene name='User:Fadel_A._Samatey/Workbench/I3DC-1/Flhb_st/6'>restore initial scene</scene>). As explained in the publication, the position of the long alpha helix appears to be stabilized by | ||
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====Comparison==== | ====Comparison==== | ||
| - | The FlhBc ''Salmonella'' <!--<scene name='User:Fadel_A._Samatey/Workbench/I3DC-1/Flhb_st_aa_aligned/2'>-->3D structure is very similar | + | The FlhBc ''Salmonella'' <!--<scene name='User:Fadel_A._Samatey/Workbench/I3DC-1/Flhb_st_aa_aligned/2'>-->3D structure is very similar to that of ''Aquifex''. 102 alpha carbons align with an RMSD of 1.0 Å. Their FlhB's have 32% sequence identity. |
<scene name='User:Fadel_A._Samatey/FlhBc_I/Flhbc_st_plus_aa/2'>Display both structures</scene>, then click the button below to do a structural alignment. | <scene name='User:Fadel_A._Samatey/FlhBc_I/Flhbc_st_plus_aa/2'>Display both structures</scene>, then click the button below to do a structural alignment. | ||
<jmol> | <jmol> | ||
Revision as of 13:09, 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
