Motion in T7 Phage RNA Polymerase [t7rnapol]
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Classification [D-h-2]
Structures 1ARO with lysozyme 1CEZ promoter complex 1QLN initiation complex 1MSQ elongation complex
Description The N-terminal domain undergoes a massive change in tertiary structure during the transition from initiation to elongation phase, involving a 70 Angstrom movement of one domain. This refolding opens an exit tunnel for the seven-nucleotide mRNA chain, which would otherwise be sterically blocked in the initiation complex.
References Yin YW, Steitz TA (2002). Structural basis for the transition from initiation to elongation transcription in T7 RNA p olymerase. Science 298:1387-95. [Medline info for 12242451] Cheetham GM, Steitz TA (1999). Structure of a transcribing T7 RNA polymerase initiation complex. Science 286:2305-9. [Medline info for 10600732] G M Cheetham, D Jeruzalmi, T A Steitz (1999). Structural basis for initiation of transcription from an RNA polymerase-promoter complex. Nature, 399:80-3 [Medline info for 10331394] D Jeruzalmi, T A Steitz (1998). Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme. EMBO J, 17:4101-13 [Medline info for 9670025]
GO terms associated with structures Molecular function DNA binding, DNA-directed RNA polymerase activity, N-acetylmuramoyl-L-alanine amidase activity Biological process transcription, peptidoglycan catabolism
Morphs
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Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]
Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu