User:Fadel A. Samatey/FlhBc I

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(Molecular Tour: FlhBc Structures)
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<center><span style="background-color:black;color:white;padding:4px;"><b><font color="#3030ff">S</font><font color="#30a0ff">al</font><font color="#00ff80">m</font><font color="#00ff00">on</font><font color="#e0ff00">e</font><font color="#ff8000">ll</font><font color="#ff0000">a</font> <font color="#909090">vs.</font> Aquifex</b>.</span></center>
<center><span style="background-color:black;color:white;padding:4px;"><b><font color="#3030ff">S</font><font color="#30a0ff">al</font><font color="#00ff80">m</font><font color="#00ff00">on</font><font color="#e0ff00">e</font><font color="#ff8000">ll</font><font color="#ff0000">a</font> <font color="#909090">vs.</font> Aquifex</b>.</span></center>
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===Loop 281-285===
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Both FlhBc structures have a protruding loop, which in ''Salmonella'' is 281-285. Despite the fact that this loop is not conserved (see below), its deletion abolished motility. Mutation of the loop
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===References and Notes===
===References and Notes===

Revision as of 08:40, 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

Cytoplasmic domain of FlhB

Drag the structure with the mouse to rotate

References and Notes

  1. Optimum growth ~90o C.

Proteopedia Page Contributors and Editors (what is this?)

Eric Martz

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