User:Fadel A. Samatey/FlhBc I

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(Molecular Tour: FlhBc Structures)
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====''Salmonella''====
====''Salmonella''====
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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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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>).
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<center><span style="background-color:black;padding:4px;">{{Template:ColorKey_Helix}},
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{{Template:ColorKey_Strand}}</span></center>
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As explained in the publication, the position of the long alpha helix appears to be stabilized by
[[crystal contacts]] (not shown).
[[crystal contacts]] (not shown).
<!--<scene name='User:Fadel_A._Samatey/Workbench/I3DC-1/Flhb_st_xtl_contacts/2'>crystal contacts</scene> (use the ''popup'' button to see details).-->
<!--<scene name='User:Fadel_A._Samatey/Workbench/I3DC-1/Flhb_st_xtl_contacts/2'>crystal contacts</scene> (use the ''popup'' button to see details).-->

Revision as of 13:24, 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

Cytoplasmic domain of FlhB

Drag the structure with the mouse to rotate

References and Notes

  1. Optimum growth ~90o C.

Notes for Developers

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