RTP and Tus: Difference between revisions
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<scene name='colorSTRUCTURE'>structure</scene> | <scene name='colorSTRUCTURE'>structure</scene> | ||
[[Image:1ECR|300px|left|thumb| Tus-Ter complex]] | [[Image:1ECR.jpg|300px|left|thumb| Tus-Ter complex]] | ||
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. | 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. | ||
