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2hqc

From Proteopedia

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[[Image:2hqc.gif|left|200px]]
 
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{{Structure
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==Conformation of the AcrB Multidrug Efflux Pump in Mutants of the Putative Proton Relay Pathway==
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|PDB= 2hqc |SIZE=350|CAPTION= <scene name='initialview01'>2hqc</scene>, resolution 3.56&Aring;
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<StructureSection load='2hqc' size='340' side='right'caption='[[2hqc]], [[Resolution|resolution]] 3.56&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2hqc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HQC FirstGlance]. <br>
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|ACTIVITY=
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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]] 3.56&#8491;</td></tr>
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|GENE= acrB, acrE, b0462 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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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=2hqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hqc OCA], [https://pdbe.org/2hqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hqc RCSB], [https://www.ebi.ac.uk/pdbsum/2hqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hqc ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''Conformation of the AcrB Multidrug Efflux Pump in Mutants of the Putative Proton Relay Pathway'''
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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We previously reported the X-ray structures of wild-type Escherichia coli AcrB, a proton motive force-dependent multidrug efflux pump, and its N109A mutant. These structures presumably reflect the resting state of AcrB, which can bind drugs. After ligand binding, a proton may bind to an acidic residue(s) in the transmembrane domain, i.e., Asp407 or Asp408, within the putative network of electrostatically interacting residues, which also include Lys940 and Thr978, and this may initiate a series of conformational changes that result in drug expulsion. Herein we report the X-ray structures of four AcrB mutants, the D407A, D408A, K940A, and T978A mutants, in which the structure of this tight electrostatic network is expected to become disrupted. These mutant proteins revealed remarkably similar conformations, which show striking differences from the previously known conformations of the wild-type protein. For example, the loop containing Phe386 and Phe388, which play a major role in the initial binding of substrates in the central cavity, becomes prominently extended into the center of the cavity, such that binding of large substrate molecules may become difficult. We believe that this new conformation may mimic, at least partially, one of the transient conformations of the transporter during the transport cycle.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hq/2hqc_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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2HQC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HQC OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=2hqc ConSurf].
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Conformation of the AcrB multidrug efflux pump in mutants of the putative proton relay pathway., Su CC, Li M, Gu R, Takatsuka Y, McDermott G, Nikaido H, Yu EW, J Bacteriol. 2006 Oct;188(20):7290-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17015668 17015668]
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<div style="clear:both"></div>
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[[Category: Escherichia coli]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Gu, R.]]
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__TOC__
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[[Category: Li, M.]]
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</StructureSection>
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[[Category: McDermott, G.]]
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[[Category: Escherichia coli K-12]]
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[[Category: Nikaido, H.]]
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[[Category: Large Structures]]
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[[Category: Su, C C.]]
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[[Category: Gu R]]
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[[Category: Takatsuka, Y.]]
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[[Category: Li M]]
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[[Category: Yu, E W.]]
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[[Category: McDermott G]]
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[[Category: membrane protein]]
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[[Category: Nikaido H]]
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[[Category: multidrug efflux pump]]
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[[Category: Su C-C]]
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[[Category: Takatsuka Y]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:20:12 2008''
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[[Category: Yu EW]]

Current revision

Conformation of the AcrB Multidrug Efflux Pump in Mutants of the Putative Proton Relay Pathway

PDB ID 2hqc

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