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 functionDNA binding, DNA-directed RNA polymerase activity, N-acetylmuramoyl-L-alanine amidase activity
Biological processtranscription, peptidoglycan catabolism

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu