Sandbox20: Difference between revisions
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=The Proteins= | =The Proteins= | ||
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===DNA Binding=== | ===DNA Binding=== | ||
13-15 residues contribute to the attachment of an RTP molecule to the ''Ter'' | 13-15 residues contribute to the attachment of an RTP molecule to the ''Ter'' DNA site. Most of this is contributed by the basic residues of the <scene name='Sandbox20/2efw/30'>α3 helix</scene>, which lies in the major groove of DNA. | ||
The asymmetry of the dimer is shown by the names 'wing up' and 'wing down'. It is measured by the angle between the a2 and a3 heices, as shown <scene name='Sandbox20/2efw/14'>by clicking here</scene>. | The asymmetry of the dimer is shown by the names 'wing up' and 'wing down'. It is measured by the angle between the a2 and a3 heices, as shown <scene name='Sandbox20/2efw/14'>by clicking here</scene>. | ||
=== Replication Termination Activity=== | === Replication Termination Activity=== | ||
The consequence of these different conformations is most prominent in the position of the B1 sheet. This is evident in the Tyr33 residue, <scene name='Sandbox20/2efw/20'>shown by clicking here</scene> | |||
Space, which contact DNA only in the wing-down conformation. | |||
Space | |||
==Tus== | ==Tus== | ||