1pea

<StructureSection load='1pea' size='340' side='right' caption='[[1pea]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[1pea]] is a 1 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=1PEA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PEA FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACM:ACETAMIDE'>ACM</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=1pea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pea OCA], [http://pdbe.org/1pea PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pea RCSB], [http://www.ebi.ac.uk/pdbsum/1pea PDBsum]</span></td></tr>

[[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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pe/1pea_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

The crystal structure for the negative regulator (AmiC) of the amidase operon from Pseudomonas aeruginosa has been solved at a resolution of 2.1 A. AmiC is the amide sensor protein in the amidase operon and regulates the activity of the transcription antitermination factor AmiR, which in turn regulates amidase expression. The AmiC structure consists of two domains with an alternating beta-alpha-beta topology. The two domains are separated by a central cleft and the amide binding site is positioned in this cleft at the interface of the domains. The overall fold for AmiC is extremely similar to that for the leucine-isoleucine-valine binding protein (LivJ) of Escherichia coli despite only 17% sequence identity, however, the two domains of AmiC are substantially closed compared with LivJ. The closed structure of AmiC is stabilized significantly by the bound acetamide, suggesting a molecular mechanism for the process of amide induction. The amide binding site is extremely specific for acetamide and would not allow a closed conformation in the presence of the anti-inducer molecule butyramide.

Crystal structure of AmiC: the controller of transcription antitermination in the amidase operon of Pseudomonas aeruginosa.,Pearl L, O'Hara B, Drew R, Wilson S EMBO J. 1994 Dec 15;13(24):5810-7. PMID:7813419<ref>PMID:7813419</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1pea" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Hara, B P.O]]

[[Category: Pearl, L H]]

[[Category: Binding protein]]

[[Category: Gene regulator]]

[[Category: Receptor]]