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      Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution.

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          Abstract

          Structures of a 10-subunit yeast RNA polymerase II have been derived from two crystal forms at 2.8 and 3.1 angstrom resolution. Comparison of the structures reveals a division of the polymerase into four mobile modules, including a clamp, shown previously to swing over the active center. In the 2.8 angstrom structure, the clamp is in an open state, allowing entry of straight promoter DNA for the initiation of transcription. Three loops extending from the clamp may play roles in RNA unwinding and DNA rewinding during transcription. A 2.8 angstrom difference Fourier map reveals two metal ions at the active site, one persistently bound and the other possibly exchangeable during RNA synthesis. The results also provide evidence for RNA exit in the vicinity of the carboxyl-terminal repeat domain, coupling synthesis to RNA processing by enzymes bound to this domain.

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          Author and article information

          Journal
          Science
          Science (New York, N.Y.)
          American Association for the Advancement of Science (AAAS)
          0036-8075
          0036-8075
          Jun 08 2001
          : 292
          : 5523
          Affiliations
          [1 ] Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.
          Article
          1059493
          10.1126/science.1059493
          11313498
          e3d83ae1-81d0-4518-b9b3-e848ab84ea5e
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