1ARO
T7 RNA POLYMERASE COMPLEXED WITH T7 LYSOZYME
Summary for 1ARO
| Entry DOI | 10.2210/pdb1aro/pdb |
| Descriptor | T7 RNA POLYMERASE, T7 LYSOZYME, MERCURY (II) ION (3 entities in total) |
| Functional Keywords | transcription, dna-directed rna polymerase, hydrolase, glycosidase, complex (polymerase-hydrolase), complex (polymerase-hydrolase) complex, complex (polymerase/hydrolase) |
| Biological source | Enterobacteria phage T7 More |
| Total number of polymer chains | 2 |
| Total formula weight | 117347.48 |
| Authors | Steitz, T.,Jeruzalmi, D. (deposition date: 1997-08-08, release date: 1998-10-21, Last modification date: 2024-02-07) |
| Primary citation | Jeruzalmi, D.,Steitz, T.A. Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme. EMBO J., 17:4101-4113, 1998 Cited by PubMed Abstract: 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. PubMed: 9670025DOI: 10.1093/emboj/17.14.4101 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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