User:Fadel A. Samatey/FlhBc I

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(Molecular Tour: FlhBc Structures)
(Molecular Tour: FlhBc Structures)
Line 44: Line 44:
===Flexibility of N-Terminus===
===Flexibility of N-Terminus===
-
Molecular dynamics simulations suggested that the mutations in 281-285 reduced flexibility of the N-terminal alpha helix, and hence that such flexibility may be important for function. Indeed, 226-267 (the N-terminal helix) is predicted to be intrinsically disordered<ref><img src='Image:3b0z-FlhB-Foldindex.png'</ref>. The formation of a helix seems likely to be the result of stabilization by crystal contacts mentioned above.
+
Molecular dynamics simulations suggested that the mutations in 281-285 reduced flexibility of the N-terminal alpha helix, and hence that such flexibility may be important for function. Indeed, 226-267 (the N-terminal helix) is predicted to be intrinsically disordered<ref><img src='Image:3b0z-FlhB-Foldindex.png'></ref>. The formation of a helix seems likely to be the result of stabilization by crystal contacts mentioned above.
</StructureSection>
</StructureSection>
===References and Notes===
===References and Notes===

Revision as of 09:44, 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.
  2. <img src='Image:3b0z-FlhB-Foldindex.png'>

Proteopedia Page Contributors and Editors (what is this?)

Eric Martz

Personal tools