1QO0
Amide receptor of the amidase operon of Pseudomonas aeruginosa (AmiC) complexed with the negative regulator AmiR.
Summary for 1QO0
| Entry DOI | 10.2210/pdb1qo0/pdb |
| Related | 1PEA 1QNL |
| Descriptor | AMIC, AMIR, BUTYRAMIDE, ... (4 entities in total) |
| Functional Keywords | binding protein, gene regulator, receptor |
| Biological source | PSEUDOMONAS AERUGINOSA More |
| Total number of polymer chains | 4 |
| Total formula weight | 129900.88 |
| Authors | Pearl, L.H.,O'Hara, B.P.,Roe, S.M. (deposition date: 1999-10-26, release date: 1999-12-23, Last modification date: 2023-12-13) |
| Primary citation | O'Hara, B.P.,Norman, R.A.,Wan, P.T.C.,Roe, S.M.,Barrett, T.E.,Drew, R.E.,Pearl, L.H. Crystal Structure and Induction Mechanism of Amic-Amir: A Ligand-Regulated Transcription Antitermination Complex Embo J., 18:5175-, 1999 Cited by PubMed Abstract: Inducible expression of the aliphatic amidase operon in Pseudomonas aeruginosa is controlled by an antitermination mechanism which allows production of the full-length transcript only in the presence of small-molecule inducers, such as acetamide. Ligand-regulated antitermination is provided by AmiC, the ligand-sensitive negative regulator, and AmiR, the RNA-binding positive regulator. Under non-inducing or repressing growth conditions, AmiC and AmiR form a complex in which the activity of AmiR is silenced. The crystal structure of the AmiC-AmiR complex identifies AmiR as a new and highly unusual member of the response-regulator family of bacterial signal transduction proteins, regulated by sequestration rather than phosphorylation. Comparison with the structure of free AmiC reveals the subtle mechanism of ligand-induced release of AmiR. PubMed: 10508151DOI: 10.1093/EMBOJ/18.19.5175 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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