Sandbox Reserved 1659: Difference between revisions

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[[Image:pymol1.jpg]].

The flexibility of H4 and H5 may have a role in the binding to BADH1. Furthermore, <scene name='86/868192/The_lysine_180_and_181/1'>~~Text To Be Displayed~~</scene> are placed on this H5 helix, and they are responsible for the ligation to BAHD1 so it can cause a conformational change. Many amino acids may be involved in the interaction of LntA with its ligand, such as BAHD1. A <scene name='86/868192/Dilysine/1'>dilysine motif located in the elbow region of lntA at position 180/181</scene> has proven to be essential for the interaction with the transcription factor BAHD1. Indeed, when this motif is substituted by two aspartic acid amino acids (K180D/K181D by mutation of LntA), a local redistribution of the charges is observed and lntA is not able anymore to interact with BAHD1. <ref> Lebreton A, Job V, Ragon M, Le Monnier A, Dessen A, Cossart P, Bierne H. 2014. Structural basis for the inhibition of the chromatin repressor BAHD1 by the bacterial nucleomodulin LntA </ref>

The flexibility of H4 and H5 may have a role in the binding to BADH1. Furthermore, <scene name='86/868192/The_lysine_180_and_181/1'>the lysine 180 and 181</scene> are placed on this H5 helix, and they are responsible for the ligation to BAHD1 so it can cause a conformational change. Many amino acids may be involved in the interaction of LntA with its ligand, such as BAHD1. A <scene name='86/868192/Dilysine/1'>dilysine motif located in the elbow region of lntA at position 180/181</scene> has proven to be essential for the interaction with the transcription factor BAHD1. Indeed, when this motif is substituted by two aspartic acid amino acids (K180D/K181D by mutation of LntA), a local redistribution of the charges is observed and lntA is not able anymore to interact with BAHD1. <ref> Lebreton A, Job V, Ragon M, Le Monnier A, Dessen A, Cossart P, Bierne H. 2014. Structural basis for the inhibition of the chromatin repressor BAHD1 by the bacterial nucleomodulin LntA </ref>

Third patch has other charged residues which are likely to play a role in the interaction but they are less conserved so they might not be absolutely essential to the formation of the BAHD1-lntA complex.

This protein can also be stabilized by glycerol molecules because they are hydrophobic and it prevents hydrolyzation. (green link)

Sandbox Reserved 1659: Difference between revisions

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@@ Line 22: / Line 22: @@
 [[Image:pymol1.jpg]].
-The flexibility of H4 and H5 may have a role in the binding to BADH1. Furthermore, <scene name='86/868192/The_lysine_180_and_181/1'>Text To Be Displayed</scene> are placed on this H5 helix, and they are responsible for the ligation to BAHD1 so it can cause a conformational change. Many amino acids may be involved in the interaction of LntA with its ligand, such as BAHD1. A <scene name='86/868192/Dilysine/1'>dilysine motif located in the elbow region of lntA at position 180/181</scene> has proven to be essential for the interaction with the transcription factor BAHD1. Indeed, when this motif is substituted by two aspartic acid amino acids (K180D/K181D by mutation of LntA), a local redistribution of the charges is observed and lntA is not able anymore to interact with BAHD1. <ref> Lebreton A, Job V, Ragon M, Le Monnier A, Dessen A, Cossart P, Bierne H. 2014. Structural basis for the inhibition of the chromatin repressor BAHD1 by the bacterial nucleomodulin LntA </ref>
+The flexibility of H4 and H5 may have a role in the binding to BADH1. Furthermore, <scene name='86/868192/The_lysine_180_and_181/1'>the lysine 180 and 181</scene> are placed on this H5 helix, and they are responsible for the ligation to BAHD1 so it can cause a conformational change. Many amino acids may be involved in the interaction of LntA with its ligand, such as BAHD1. A <scene name='86/868192/Dilysine/1'>dilysine motif located in the elbow region of lntA at position 180/181</scene> has proven to be essential for the interaction with the transcription factor BAHD1. Indeed, when this motif is substituted by two aspartic acid amino acids (K180D/K181D by mutation of LntA), a local redistribution of the charges is observed and lntA is not able anymore to interact with BAHD1. <ref> Lebreton A, Job V, Ragon M, Le Monnier A, Dessen A, Cossart P, Bierne H. 2014. Structural basis for the inhibition of the chromatin repressor BAHD1 by the bacterial nucleomodulin LntA </ref>
 Third patch has other charged residues which are likely to play a role in the interaction but they are less conserved so they might not be absolutely essential to the formation of the BAHD1-lntA complex.
 This protein can also be stabilized by glycerol molecules because they are hydrophobic and it prevents hydrolyzation. (green link)