Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme.,Jeruzalmi D, Steitz TA EMBO J. 1998 Jul 15;17(14):4101-13. PMID:9670025[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jeruzalmi D, Steitz TA. Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme. EMBO J. 1998 Jul 15;17(14):4101-13. PMID:9670025 doi:10.1093/emboj/17.14.4101