1UNK
STRUCTURE OF COLICIN E7 IMMUNITY PROTEIN
Summary for 1UNK
| Entry DOI | 10.2210/pdb1unk/pdb |
| Descriptor | COLICIN E7 (2 entities in total) |
| Functional Keywords | immunity protein, dimeric structure, rnase active site |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 39627.85 |
| Authors | Ko, T.-P.,Hsieh, S.-Y.,Ku, W.-Y.,Tseng, M.-Y.,Chak, K.-F.,Yuan, H.S. (deposition date: 1996-06-21, release date: 1998-01-07, Last modification date: 2024-02-14) |
| Primary citation | Hsieh, S.Y.,Ko, T.P.,Tseng, M.Y.,Ku, W.,Chak, K.F.,Yuan, H.S. A novel role of ImmE7 in the autoregulatory expression of the ColE7 operon and identification of possible RNase active sites in the crystal structure of dimeric ImmE7. EMBO J., 16:1444-1454, 1997 Cited by PubMed Abstract: Site-specific cleavage of mRNA has been identified in vivo for the polycistronic colicin E7 operon (ColE7), which occurs between G and A nucleotides located at the Asp52 codon (GAT) of the immunity gene (ceiE7). In vitro, this specific cleavage occurs only in the presence of the ceiE7 gene product (ImmE7). The crystal structure of dimeric ImmE7 has been determined at 1.8 A resolution by X-ray crystallographic analysis. We found that several residues located at the interface of dimeric ImmE7 bear surprising resemblance to the active sites of some RNases. These results suggest that dimeric ImmE7 may possess a novel RNase activity that cleaves its own mRNA at a specific site and thus autoregulates translational expression of the downstream celE7 gene as well as degradation of the upstream ceaE7 mRNA. PubMed: 9135159DOI: 10.1093/emboj/16.6.1444 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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