Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme.
The T7 RNA polymerase-T7 lysozyme complex regulates phage gene expression during infection of Escherichia coli. The 2.8 A crystal structure of the complex reveals that lysozyme binds at a site remote from the polymerase active site, suggesting an indirect mechanism of inhibition. Comparison of the T7 RNA polymerase structure with that of the homologous pol I family of DNA polymerases reveals identities in the catalytic site but also differences specific to RNA polymerase function. The structure of T7 RNA polymerase presented here differs significantly from a previously published structure. Sequence similarities between phage RNA polymerases and those from mitochondria and chloroplasts, when interpreted in the context of our revised model of T7 RNA polymerase, suggest a conserved fold.[1]References
- Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme. Jeruzalmi, D., Steitz, T.A. EMBO J. (1998) [Pubmed]
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