2gfp

<StructureSection load='2gfp' size='340' side='right' caption='[[2gfp]], [[Resolution|resolution]] 3.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[2gfp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The November 2007 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Multidrug Resistance Transporters'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2007_11 10.2210/rcsb_pdb/mom_2007_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GFP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GFP FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">emrD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=2gfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gfp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gfp RCSB], [http://www.ebi.ac.uk/pdbsum/2gfp PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gf/2gfp_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

EmrD is a multidrug transporter from the Major Facilitator Superfamily that expels amphipathic compounds across the inner membrane of Escherichia coli. Here, we report the x-ray structure of EmrD determined to a resolution of 3.5 angstroms. The structure reveals an interior that is composed mostly of hydrophobic residues, which is consistent with its role transporting amphipathic molecules. Two long loops extend into the inner leaflet side of the cell membrane. This region can serve to recognize and bind substrate directly from the lipid bilayer. We propose that multisubstrate specificity, binding, and transport are facilitated by these loop regions and the internal cavity.

Structure of the multidrug transporter EmrD from Escherichia coli.,Yin Y, He X, Szewczyk P, Nguyen T, Chang G Science. 2006 May 5;312(5774):741-4. PMID:16675700<ref>PMID:16675700</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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==See Also==

*[[Major Facilitators|Major Facilitators]]

== References ==

<references/>

[[Category: Chang, G.]]

[[Category: He, X.]]

[[Category: Nguyen, T.]]

[[Category: Szewczyk, P.]]

[[Category: Yin, Y.]]

[[Category: Multidrug transporter]]