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RTP and Tus
From Proteopedia
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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> | ||
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| + | [[Image:1ECR|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. | ||
Revision as of 01:52, 13 May 2011
A comparison of the Replication Terminator Protein (from Bacillus subtillis) and Tus (from Escerishia coli) provides an interesting insight into how proteins with vastly different structures and mechanisms of action can produce essentially identical effects in their native systems.
Looking at the structures of these two proteins, it is not immediately obvious that they would perfom the same function, specifically, to arrest the progression of the replication fork along the bacterial chromosome at specific sites (termed Ter sites). Furthermore, this arrest-mechanism functions in a polar manner in both organisms, which is perhaps surprising considering the symmetrical characteristics of both proteins.
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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.
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