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The structure of a transcribing T7 RNA polymerase in transition from initiation to elongation
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The crystal structures of T7 RNAP bound to substrate DNA and either a 7 nt or 8 nt transcript are described. They show a 40° and 45° rotation of the promoter binding domains resulting in an enlargement of the heteroduplex product binding cleft. They represent intermediate states in the transition from the initiation to elongation states.
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Durniak K., Bailey S., and Steitz T.A. The structure of a transcribing T7 RNA polymerase in transition from initiation to elongation. Science 322 (2008) 553-557. The crystal structures of T7 RNAP bound to substrate DNA and either a 7 nt or 8 nt transcript are described. They show a 40° and 45° rotation of the promoter binding domains resulting in an enlargement of the heteroduplex product binding cleft. They represent intermediate states in the transition from the initiation to elongation states.
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These structures of ternary complex of phi29 DNA polymerase show conformational changes in the fingers domain of this B-family polymerase that are analogous to those of the A-family polymerases.
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The specificity loop of T7 RNA polymerase interacts first with the promoter and then with the elongating transcript, suggesting a mechanism for promoter clearance
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Probing conformational changes in T7 RNA polymerase during initiation and termination by using engineered disulfide crosslinks
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