2qop

<StructureSection load='2qop' size='340' side='right' caption='[[2qop]], [[Resolution|resolution]] 2.55&Aring;' scene=''>

<table><tr><td colspan='2'>[[2qop]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QOP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QOP FirstGlance]. <br>

</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=2qop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qop OCA], [http://pdbe.org/2qop PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qop RCSB], [http://www.ebi.ac.uk/pdbsum/2qop PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/ACRR_ECOLI ACRR_ECOLI]] Potential regulator protein for the acrAB genes.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qo/2qop_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 AcrAB multidrug efflux pump, which belongs to the resistance nodulation division (RND) family, recognizes and extrudes a wide range of antibiotics and chemotherapeutic agents and causes the intrinsic antibiotic resistance in Escherichia coli. The expression of AcrAB is controlled by the transcriptional regulator AcrR, whose open reading frame is located 141 bp upstream of the acrAB operon. To understand the structural basis of AcrR regulation, we have determined the crystal structure of AcrR to 2.55-A resolution, revealing a dimeric two-domain molecule with an entirely helical architecture similar to members of the TetR family of transcriptional regulators. Each monomer of AcrR forms a multientrance pocket of 350 A(3) in the ligand-binding domain. The ligand-binding pocket is surrounded with mostly hydrophobic residues. In addition, a completely buried negatively charged glutamate, expected to be critical for drug binding, is located at the center of the binding pocket. The crystal structure provides novel insight into the mechanisms of ligand binding and AcrR regulation.

Crystal structure of the transcriptional regulator AcrR from Escherichia coli.,Li M, Gu R, Su CC, Routh MD, Harris KC, Jewell ES, McDermott G, Yu EW J Mol Biol. 2007 Nov 30;374(3):591-603. Epub 2007 Sep 29. PMID:17950313<ref>PMID:17950313</ref>

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== References ==

[[Category: Ecoli]]

[[Category: Gu, R]]

[[Category: Li, M]]

[[Category: McDermott, G]]

[[Category: Su, C C]]

[[Category: Yu, E W]]

[[Category: Transcription regulation]]