User:Fadel A. Samatey/FlhBc I: Difference between revisions

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===Loop 281-285===

Both FlhBc structures have a <scene name='User:Fadel_A._Samatey/FlhBc_I/281-285/2'>protruding loop, which in ''Salmonella'' is 281-285, ENKMS</scene>. Despite the fact that this loop is '''not conserved''' (see below), its deletion abolished motility. Mutation of the loop to PPPPP reduced motility, while mutation to AAAAA had no effect. The reductions in motility correlated with reductions in secretion of hook protein FlgE and filament protein FliC. Molecular dynamics simulations suggested that the mutations ~~reduce~~ flexibility of the N-terminal alpha helix, and hence that such flexibility may be important for function.

Both FlhBc structures have a <scene name='User:Fadel_A._Samatey/FlhBc_I/281-285/3'>protruding loop, which in ''Salmonella'' is 281-285, ENKMS</scene>. Despite the fact that this loop is '''not conserved''' (see below), its deletion abolished motility. Mutation of the loop to PPPPP reduced motility, while mutation to AAAAA had no effect. The reductions in motility correlated with reductions in secretion of hook protein FlgE and filament protein FliC.

===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. The formation of a helix seems likely to be the result of stabilization by crystal contacts mentioned above.

</StructureSection>

===References and Notes===

@@ Line 41: / Line 41: @@
 ===Loop 281-285===
-Both FlhBc structures have a <scene name='User:Fadel_A._Samatey/FlhBc_I/281-285/2'>protruding loop, which in ''Salmonella'' is 281-285, ENKMS</scene>. Despite the fact that this loop is '''not conserved''' (see below), its deletion abolished motility. Mutation of the loop to PPPPP reduced motility, while mutation to AAAAA had no effect. The reductions in motility correlated with reductions in secretion of hook protein FlgE and filament protein FliC. Molecular dynamics simulations suggested that the mutations reduce flexibility of the N-terminal alpha helix, and hence that such flexibility may be important for function.
+Both FlhBc structures have a <scene name='User:Fadel_A._Samatey/FlhBc_I/281-285/3'>protruding loop, which in ''Salmonella'' is 281-285, ENKMS</scene>. Despite the fact that this loop is '''not conserved''' (see below), its deletion abolished motility. Mutation of the loop to PPPPP reduced motility, while mutation to AAAAA had no effect. The reductions in motility correlated with reductions in secretion of hook protein FlgE and filament protein FliC.
+===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. The formation of a helix seems likely to be the result of stabilization by crystal contacts mentioned above.
 </StructureSection>
 ===References and Notes===