Sandbox20: Difference between revisions
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=The Proteins= | =The Proteins= | ||
==RTP== | |||
<Structure load='2EFW' size='300' frame='true' align='right' caption='RTP' scene='Sandbox20/2efw/3' /> | <Structure load='2EFW' size='300' frame='true' align='right' caption='RTP' scene='Sandbox20/2efw/3' /> | ||
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Space | Space | ||
==Tus== | |||
<Structure load='2EWJ' size='300' frame='true' align='right' caption='Tus' scene='Sandbox20/Tus/2' /> | <Structure load='2EWJ' size='300' frame='true' align='right' caption='Tus' scene='Sandbox20/Tus/2' /> | ||
This is the area for text about Tus | This is the area for text about Tus. | ||
===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." | "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> | 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. |