3b62: Difference between revisions

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==EmrE multidrug transporter in complex with P4P, P21 crystal form==
==EmrE multidrug transporter in complex with P4P, P21 crystal form==
<StructureSection load='3b62' size='340' side='right' caption='[[3b62]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
<StructureSection load='3b62' size='340' side='right'caption='[[3b62]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3b62]] is a 4 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=3B62 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3B62 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3b62]] is a 4 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=3B62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B62 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P4P:TETRAPHENYLPHOSPHONIUM'>P4P</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]] 4.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3b5d|3b5d]], [[3b61|3b61]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P4P:TETRAPHENYLPHOSPHONIUM'>P4P</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">emrE, eb, mvrC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3b62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b62 OCA], [https://pdbe.org/3b62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b62 RCSB], [https://www.ebi.ac.uk/pdbsum/3b62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b62 ProSAT]</span></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=3b62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b62 OCA], [http://pdbe.org/3b62 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3b62 RCSB], [http://www.ebi.ac.uk/pdbsum/3b62 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/EMRE_ECOLI EMRE_ECOLI]] Multidrug transporter that expels positively charged hydrophobic drugs across the inner membrane of E.coli., thereby conferring resistance to a wide range of toxic compounds. The drug efflux is coupled to an influx of protons. Is involved in the resistance of E.coli cells to methyl viologen, ethidium bromide and acriflavine. Is also able to transport tetraphenylphosphonium (TPP(+)) and benzalkonium.<ref>PMID:7896833</ref> <ref>PMID:10681497</ref> <ref>PMID:15371426</ref>
[https://www.uniprot.org/uniprot/EMRE_ECOLI EMRE_ECOLI] Multidrug transporter that expels positively charged hydrophobic drugs across the inner membrane of E.coli., thereby conferring resistance to a wide range of toxic compounds. The drug efflux is coupled to an influx of protons. Is involved in the resistance of E.coli cells to methyl viologen, ethidium bromide and acriflavine. Is also able to transport tetraphenylphosphonium (TPP(+)) and benzalkonium.<ref>PMID:7896833</ref> <ref>PMID:10681497</ref> <ref>PMID:15371426</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b6/3b62_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b6/3b62_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 20: Line 20:
</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=3b62 ConSurf].
</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=3b62 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
EmrE, a multidrug transporter from Escherichia coli, functions as a homodimer of a small four-transmembrane protein. The membrane insertion topology of the two monomers is controversial. Although the EmrE protein was reported to have a unique orientation in the membrane, models based on electron microscopy and now defunct x-ray structures, as well as recent biochemical studies, posit an antiparallel dimer. We have now reanalyzed our x-ray data on EmrE. The corrected structures in complex with a transport substrate are highly similar to the electron microscopy structure. The first three transmembrane helices from each monomer surround the substrate binding chamber, whereas the fourth helices participate only in dimer formation. Selenomethionine markers clearly indicate an antiparallel orientation for the monomers, supporting a "dual topology" model.
X-ray structure of EmrE supports dual topology model.,Chen YJ, Pornillos O, Lieu S, Ma C, Chen AP, Chang G Proc Natl Acad Sci U S A. 2007 Nov 27;104(48):18999-9004. Epub 2007 Nov, 16. PMID:18024586<ref>PMID:18024586</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3b62" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Chang, G]]
[[Category: Large Structures]]
[[Category: Chen, Y J]]
[[Category: Chang G]]
[[Category: Antiport]]
[[Category: Chen YJ]]
[[Category: Helical membrane protein]]
[[Category: Inner membrane]]
[[Category: Membrane protein]]
[[Category: Multidrug resistance transporter]]
[[Category: Smr]]
[[Category: Transmembrane]]

Latest revision as of 09:27, 21 February 2024

EmrE multidrug transporter in complex with P4P, P21 crystal form

3b62, resolution 4.40Å

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