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| | <StructureSection load='1qo0' size='340' side='right'caption='[[1qo0]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='1qo0' size='340' side='right'caption='[[1qo0]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qo0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QO0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qo0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QO0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMD:BUTYRAMIDE'>BMD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pea|1pea]], [[1qnl|1qnl]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMD:BUTYRAMIDE'>BMD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qo0 OCA], [http://pdbe.org/1qo0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qo0 RCSB], [http://www.ebi.ac.uk/pdbsum/1qo0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qo0 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qo0 OCA], [https://pdbe.org/1qo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qo0 RCSB], [https://www.ebi.ac.uk/pdbsum/1qo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qo0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AMIC_PSEAE AMIC_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. [[http://www.uniprot.org/uniprot/AMIR_PSEAE AMIR_PSEAE]] Positive controlling element of AmiE, the gene for aliphatic amidase. Acts as a transcriptional antitermination factor. It is thought to allow RNA polymerase read through a rho-independent transcription terminator between the AmiE promoter and gene. | + | [https://www.uniprot.org/uniprot/AMIC_PSEAE AMIC_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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hara, B P.O]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Pearl, L H]] | + | [[Category: O'Hara BP]] |
| - | [[Category: Roe, S M]] | + | [[Category: Pearl LH]] |
| - | [[Category: Binding protein]] | + | [[Category: Roe SM]] |
| - | [[Category: Gene regulator]]
| + | |
| - | [[Category: Receptor]]
| + | |
| Structural highlights
Function
AMIC_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 PubMed
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.
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
- ↑ O'Hara BP, Norman RA, Wan PT, Roe SM, Barrett TE, Drew RE, Pearl LH. Crystal structure and induction mechanism of AmiC-AmiR: a ligand-regulated transcription antitermination complex. EMBO J. 1999 Oct 1;18(19):5175-86. PMID:10508151 doi:http://dx.doi.org/10.1093/emboj/18.19.5175
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