2i68

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{{STRUCTURE_2i68| PDB=2i68 | SCENE= }}
{{STRUCTURE_2i68| PDB=2i68 | SCENE= }}
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'''Cryo-EM based theoretical model structure of transmembrane domain of the multidrug-resistance antiporter from E. coli EmrE'''
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===Cryo-EM based theoretical model structure of transmembrane domain of the multidrug-resistance antiporter from E. coli EmrE===
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==Overview==
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Small multidrug resistance (SMR) transporters contribute to bacterial resistance by coupling the efflux of a wide range of toxic aromatic cations, some of which are commonly used as antibiotics and antiseptics, to proton influx. EmrE is a prototypical small multidrug resistance transporter comprising four transmembrane segments (M1-M4) that forms dimers. It was suggested recently that EmrE molecules in the dimer have different topologies, i.e. monomers have opposite orientations with respect to the membrane plane. A 3-D structure of EmrE acquired by electron cryo-microscopy (cryo-EM) at 7.5 Angstroms resolution in the membrane plane showed that parts of the structure are related by quasi-symmetry. We used this symmetry relationship, combined with sequence conservation data, to assign the transmembrane segments in EmrE to the densities seen in the cryo-EM structure. A C alpha model of the transmembrane region was constructed by considering the evolutionary conservation pattern of each helix. The model is validated by much of the biochemical data on EmrE with most of the positions that were identified as affecting substrate translocation being located around the substrate-binding cavity. A suggested mechanism for proton-coupled substrate translocation in small multidrug resistance antiporters provides a mechanistic rationale to the experimentally observed inverted topology.
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{{ABSTRACT_PUBMED_17005200}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Quasi-symmetry in the cryo-EM structure of EmrE provides the key to modeling its transmembrane domain., Fleishman SJ, Harrington SE, Enosh A, Halperin D, Tate CG, Ben-Tal N, J Mol Biol. 2006 Nov 17;364(1):54-67. Epub 2006 Aug 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17005200 17005200]
Quasi-symmetry in the cryo-EM structure of EmrE provides the key to modeling its transmembrane domain., Fleishman SJ, Harrington SE, Enosh A, Halperin D, Tate CG, Ben-Tal N, J Mol Biol. 2006 Nov 17;364(1):54-67. Epub 2006 Aug 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17005200 17005200]
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Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer., Ubarretxena-Belandia I, Baldwin JM, Schuldiner S, Tate CG, EMBO J. 2003 Dec 1;22(23):6175-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14633977 14633977]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Transmembrane protein]]
[[Category: Transmembrane protein]]
[[Category: Transporter]]
[[Category: Transporter]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:28:30 2008''

Revision as of 01:28, 29 July 2008

Image:2i68.png

Template:STRUCTURE 2i68

Cryo-EM based theoretical model structure of transmembrane domain of the multidrug-resistance antiporter from E. coli EmrE

Template:ABSTRACT PUBMED 17005200

About this Structure

2I68 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Quasi-symmetry in the cryo-EM structure of EmrE provides the key to modeling its transmembrane domain., Fleishman SJ, Harrington SE, Enosh A, Halperin D, Tate CG, Ben-Tal N, J Mol Biol. 2006 Nov 17;364(1):54-67. Epub 2006 Aug 30. PMID:17005200

Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer., Ubarretxena-Belandia I, Baldwin JM, Schuldiner S, Tate CG, EMBO J. 2003 Dec 1;22(23):6175-81. PMID:14633977

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