Sandbox20: Difference between revisions

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=The Proteins=

===RTP===

==RTP==

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Space

===Tus===

==Tus==

This is the area for text about Tus~~. Original picture is <scene name='Sandbox20/Tus/2'>shown by clicking here</scene>~~.

This is the area for text about Tus.

~~Tus binds to a conserved cytosine residue which~~ is ~~not base paired <scene name='Sandbox20/Tus/13'>as shown by clicking here</scene>. The interactions between residues of the Tus protein and this unpaired cytosine nucleotide are~~ <scene name='Sandbox20/Tus/9'>shown by clicking here</scene>.

===Structural Overview===

Original picture is <scene name='Sandbox20/Tus/2'>shown by clicking here</scene>.

===DNA Binding===

Tus binds by an interaction between beta sheets (shown in green) and the major groove of DNA. This is <scene name='Sandbox20/Tus/19'>shown here</scene>

===Anti-helicase Activity===

Tus binds to a conserved cytosine residue which is not base paired <scene name='Sandbox20/Tus/13'>as shown by clicking here</scene>. The interactions between residues of the Tus protein and this unpaired cytosine nucleotide are shown in more detail <scene name='Sandbox20/Tus/9'>by clicking here</scene>.

Its ability to do this depends on the conserved glutamate residue E49.

"The crystal structure of the Tus-Ter lock shows that Glu49 of Tus makes a water-mediated hydrogen bond with the 50- phosphate of the displaced A(7) nucleotide residue, and it would thus be expected to be partially defective in formation of the locked species."

This is shown <scene name='Sandbox20/Tus/18'>by clicking here</scene>

E49K does not affect DNA binding but does affect anti-helicase activity in the ‘trapped’ complex E49 makes an indirect hydrogen bond to the phosphate of the ‘displaced’ nucleotide.

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@@ Line 22: / Line 22: @@
 =The Proteins=
-===RTP===
+==RTP==
 <Structure load='2EFW' size='300' frame='true' align='right' caption='RTP' scene='Sandbox20/2efw/3' />
@@ Line 57: / Line 57: @@
 Space
-===Tus===
+==Tus==
 <Structure load='2EWJ' size='300' frame='true' align='right' caption='Tus' scene='Sandbox20/Tus/2' />
-This is the area for text about Tus. Original picture is <scene name='Sandbox20/Tus/2'>shown by clicking here</scene>.
+This is the area for text about Tus.
-Tus binds to a conserved cytosine residue which is not base paired <scene name='Sandbox20/Tus/13'>as shown by clicking here</scene>. The interactions between residues of the Tus protein and this unpaired cytosine nucleotide are <scene name='Sandbox20/Tus/9'>shown by clicking here</scene>.
+===Structural Overview===
+Original picture is <scene name='Sandbox20/Tus/2'>shown by clicking here</scene>.
+===DNA Binding===
+Tus binds by an interaction between beta sheets (shown in green) and the major groove of DNA. This is <scene name='Sandbox20/Tus/19'>shown here</scene>
+===Anti-helicase Activity===
+Tus binds to a conserved cytosine residue which is not base paired <scene name='Sandbox20/Tus/13'>as shown by clicking here</scene>. The interactions between residues of the Tus protein and this unpaired cytosine nucleotide are shown in more detail <scene name='Sandbox20/Tus/9'>by clicking here</scene>.
+Its ability to do this depends on the conserved glutamate residue E49.
 "The crystal structure of the Tus-Ter lock shows that Glu49 of Tus makes a water-mediated hydrogen bond with the 50- phosphate of the displaced A(7) nucleotide residue, and it would thus be expected to be partially defective in formation of the locked species."
 This is shown <scene name='Sandbox20/Tus/18'>by clicking here</scene>
+E49K does not affect DNA binding but does affect anti-helicase activity in the ‘trapped’ complex E49 makes an indirect hydrogen bond to the phosphate of the ‘displaced’ nucleotide.