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3b62

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Revision as of 10:36, 25 December 2014

EmrE multidrug transporter in complex with P4P, P21 crystal form

Structural highlights

3b62 is a 4 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3b5d, 3b61
Gene:	emrE, eb, mvrC (Escherichia coli K-12)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yerushalmi H, Lebendiker M, Schuldiner S. EmrE, an Escherichia coli 12-kDa multidrug transporter, exchanges toxic cations and H+ and is soluble in organic solvents. J Biol Chem. 1995 Mar 24;270(12):6856-63. PMID:7896833
↑ Yerushalmi H, Schuldiner S. An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli. J Biol Chem. 2000 Feb 25;275(8):5264-9. PMID:10681497
↑ Rotem D, Schuldiner S. EmrE, a multidrug transporter from Escherichia coli, transports monovalent and divalent substrates with the same stoichiometry. J Biol Chem. 2004 Nov 19;279(47):48787-93. Epub 2004 Sep 15. PMID:15371426 doi:10.1074/jbc.M408187200
↑ Chen YJ, Pornillos O, Lieu S, Ma C, Chen AP, Chang G. X-ray structure of EmrE supports dual topology model. Proc Natl Acad Sci U S A. 2007 Nov 27;104(48):18999-9004. Epub 2007 Nov, 16. PMID:18024586

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3b62"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[3b62]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3B62 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P4P:TETRAPHENYLPHOSPHONIUM'>P4P</scene><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>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3b5d|3b5d]], [[3b61|3b61]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3b5d|3b5d]], [[3b61|3b61]]</td></tr>
-<tr><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 Escherichia coli K-12])</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 Escherichia coli K-12])</td></tr>
-<tr><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://www.rcsb.org/pdb/explore.do?structureId=3b62 RCSB], [http://www.ebi.ac.uk/pdbsum/3b62 PDBsum]</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://www.rcsb.org/pdb/explore.do?structureId=3b62 RCSB], [http://www.ebi.ac.uk/pdbsum/3b62 PDBsum]</span></td></tr>
-<table>
+</table>
+== 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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 33: @@
 </StructureSection>
 [[Category: Escherichia coli k-12]]
-[[Category: Chang, G.]]
+[[Category: Chang, G]]
-[[Category: Chen, Y J.]]
+[[Category: Chen, Y J]]
 [[Category: Antiport]]
 [[Category: Helical membrane protein]]

3b62

From Proteopedia

Revision as of 10:36, 25 December 2014

EmrE multidrug transporter in complex with P4P, P21 crystal form

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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