1qo0
From Proteopedia
Amide receptor of the amidase operon of Pseudomonas aeruginosa (AmiC) complexed with the negative regulator AmiR.
Structural highlights
FunctionAMIC_PSEAE Negatively regulates the expression of the aliphatic amidase operon. AmiC functions by inhibiting the action of AmiR at the protein level. It exhibits protein kinase activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedInducible 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. Crystal structure and induction mechanism of AmiC-AmiR: a ligand-regulated transcription antitermination complex.,O'Hara BP, Norman RA, Wan PT, Roe SM, Barrett TE, Drew RE, Pearl LH EMBO J. 1999 Oct 1;18(19):5175-86. PMID:10508151[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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