2rdd

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[[Image:2rdd.jpg|left|200px]]<br /><applet load="2rdd" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2rdd, resolution 3.5&Aring;" />
 
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'''X-ray crystal structure of AcrB in complex with a novel transmembrane helix.'''<br />
 
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==About this Structure==
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==X-ray crystal structure of AcrB in complex with a novel transmembrane helix.==
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2RDD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=AIC:'>AIC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RDD OCA].
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<StructureSection load='2rdd' size='340' side='right'caption='[[2rdd]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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[[Category: Escherichia coli]]
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== Structural highlights ==
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[[Category: Protein complex]]
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<table><tr><td colspan='2'>[[2rdd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RDD FirstGlance]. <br>
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[[Category: Gourdon, P.]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
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[[Category: Horsefield, R.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AIC:(2S,5R,6R)-6-{[(2R)-2-AMINO-2-PHENYLETHANOYL]AMINO}-3,3-DIMETHYL-7-OXO-4-THIA-1-AZABICYCLO[3.2.0]HEPTANE-2-CARBOXYLIC+ACID'>AIC</scene></td></tr>
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[[Category: Neutze, R.]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rdd OCA], [https://pdbe.org/2rdd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rdd RCSB], [https://www.ebi.ac.uk/pdbsum/2rdd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rdd ProSAT]</span></td></tr>
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[[Category: Tornroth-Horsefield, S.]]
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</table>
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[[Category: AIC]]
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== Function ==
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[[Category: acrb]]
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[https://www.uniprot.org/uniprot/ACRB_ECOLI ACRB_ECOLI] AcrAB is a drug efflux protein with a broad substrate specificity.<ref>PMID:16915237</ref> <ref>PMID:16946072</ref> <ref>PMID:17194213</ref>
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[[Category: antiporter]]
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== Evolutionary Conservation ==
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[[Category: drug resistance]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: inner membrane]]
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Check<jmol>
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[[Category: membrane protein]]
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<jmolCheckbox>
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[[Category: membrane protein/transport protein complex]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rd/2rdd_consurf.spt"</scriptWhenChecked>
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[[Category: multidrug efflux]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: novel transmembrane helix]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: transporter]]
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</jmolCheckbox>
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[[Category: yajc]]
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</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/main_output.php?pdb_ID=2rdd ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bacterial drug resistance is a serious concern for human health. Multidrug efflux pumps export a broad variety of substrates out of the cell and thereby convey resistance to the host. In Escherichia coli, the AcrB:AcrA:TolC efflux complex forms a principal transporter for which structures of the individual component proteins have been determined in isolation. Here, we present the X-ray structure of AcrB in complex with a single transmembrane protein, assigned by mass spectrometry as YajC. A specific rotation of the periplasmic porter domain of AcrB is also revealed, consistent with the hypothesized "twist-to-open" mechanism for TolC activation. Growth experiments with yajc-deleted E. coli reveal a modest increase in the organism's susceptibility to beta-lactam antibiotics, but this effect could not conclusively be attributed to the loss of interactions between YajC and AcrB.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:46:24 2008''
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Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist.,Tornroth-Horsefield S, Gourdon P, Horsefield R, Brive L, Yamamoto N, Mori H, Snijder A, Neutze R Structure. 2007 Dec;15(12):1663-73. PMID:18073115<ref>PMID:18073115</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2rdd" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Gourdon P]]
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[[Category: Horsefield R]]
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[[Category: Neutze R]]
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[[Category: Tornroth-Horsefield S]]

Current revision

X-ray crystal structure of AcrB in complex with a novel transmembrane helix.

PDB ID 2rdd

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