RTP and Tus: Difference between revisions
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<Structure load='1ECR' size='400' frame='true' align='right' caption='Tus complexed with Ter DNA (Kamada ''et al'' 1996)' scene='Insert optional scene name here' /> | <Structure load='1ECR' size='400' frame='true' align='right' caption='Tus complexed with Ter DNA (Kamada ''et al'' 1996)' scene='Insert optional scene name here' /> | ||
<scene name='colorSTRUCTURE'>structure</scene> | <scene name='colorSTRUCTURE'>structure</scene> | ||
The structure of Tus is unusual for a DNA-binding protein. It binds ''Ter'' DNA as an asymmetrical monomer, which establishes the basis for its polar arrest of the replication fork. Tus has three distinct regions: two α-helical regions and central β-strands which jointly form a large, positively-charged central cleft (Kamada, 1996). The core β-structres embrace 13 base pairs of duplex DNA, and at least 30 other residues make nonspecific contacts with the DNA backbone. | |||
<Structure load='1F4K' size='400' frame='true' align='left' caption='RTP complexed with ''Ter''I B-site' (Wilce ''et al'' 2001)' scene='Insert optional scene name here' /> | <Structure load='1F4K' size='400' frame='true' align='left' caption='RTP complexed with ''Ter''I B-site' (Wilce ''et al'' 2001)' scene='Insert optional scene name here' /> | ||
<scene name='colorSTRUCTURE'>structure</scene> | <scene name='colorSTRUCTURE'>structure</scene> | ||
