2gfp: Difference between revisions

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[[Image:2gfp.gif|left|200px]]<br />

[[Image:2gfp.gif|left|200px]]<br /><applet load="2gfp" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2gfp" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2gfp, resolution 3.5Å" />

'''Structure of the Multidrug Transporter EmrD from Escherichia coli'''<br />

==Overview==

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.

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.

==About this Structure==

2GFP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2GFP OCA].

2GFP is a [http://en.wikipedia.org/wiki/Single_protein 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=2GFP OCA].

==Reference==

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[[Category: membrane protein; multidrug transporter]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 18 09~~:08:~~40 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:31:15 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2gfp.gif|left|200px]]<br />
+[[Image:2gfp.gif|left|200px]]<br /><applet load="2gfp" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2gfp" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2gfp, resolution 3.5&Aring;" />
 '''Structure of the Multidrug Transporter EmrD from Escherichia coli'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-GFP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GFP OCA].
+GFP is a [http://en.wikipedia.org/wiki/Single_protein 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=2GFP OCA].
 ==Reference==
@@ Line 21: / Line 20: @@
 [[Category: membrane protein; multidrug transporter]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:08:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:31:15 2008''