3b5d
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= emrE, eb, mvrC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= emrE, eb, mvrC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b5d OCA], [http://www.ebi.ac.uk/pdbsum/3b5d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b5d RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Chang, G.]] | [[Category: Chang, G.]] | ||
[[Category: Chen, Y J.]] | [[Category: Chen, Y J.]] | ||
| - | [[Category: P4P]] | ||
[[Category: antiport]] | [[Category: antiport]] | ||
[[Category: helical membrane protein]] | [[Category: helical membrane protein]] | ||
[[Category: inner membrane]] | [[Category: inner membrane]] | ||
| - | [[Category: joint center for innovative membrane protein | + | [[Category: joint center for innovative membrane protein technologies,]] |
[[Category: multidrug resistance transporter]] | [[Category: multidrug resistance transporter]] | ||
[[Category: smr]] | [[Category: smr]] | ||
[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:23:14 2008'' |
Revision as of 02:23, 31 March 2008
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| , resolution 3.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | emrE, eb, mvrC (Escherichia coli) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
EmrE multidrug transporter in complex with TPP, C2 crystal form
Overview
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.
About this Structure
3B5D is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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