3b61
From Proteopedia
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| - | [[Image:3b61.jpg|left|200px]] | + | [[Image:3b61.jpg|left|200px]] |
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| - | '''EmrE multidrug transporter, apo crystal form''' | + | {{Structure |
| + | |PDB= 3b61 |SIZE=350|CAPTION= <scene name='initialview01'>3b61</scene>, resolution 4.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= emrE, eb, mvrC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''EmrE multidrug transporter, apo crystal form''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3B61 is a [ | + | 3B61 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=3B61 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18024586 18024586] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[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 Thu Mar 20 18:56:23 2008'' |
Revision as of 16:56, 20 March 2008
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| , resolution 4.5Å | |||||||
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| Gene: | emrE, eb, mvrC (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
EmrE multidrug transporter, apo 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
3B61 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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