2cfp: Difference between revisions

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==Overview==

Cation-coupled active transport is an essential cellular process found, ubiquitously in all living organisms. Here, we present two novel, ligand-free X-ray structures of the lactose permease (LacY) of Escherichia, coli determined at acidic and neutral pH, and propose a model for the, mechanism of coupling between lactose and H+ translocation. No, sugar-binding site is observed in the absence of ligand, and deprotonation, of the key residue Glu269 is associated with ligand binding. Thus, substrate induces formation of the sugar-binding site, as well as the, initial step in H+ transduction.

Cation-coupled active transport is an essential cellular process found ubiquitously in all living organisms. Here, we present two novel ligand-free X-ray structures of the lactose permease (LacY) of Escherichia coli determined at acidic and neutral pH, and propose a model for the mechanism of coupling between lactose and H+ translocation. No sugar-binding site is observed in the absence of ligand, and deprotonation of the key residue Glu269 is associated with ligand binding. Thus, substrate induces formation of the sugar-binding site, as well as the initial step in H+ transduction.

==About this Structure==

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[[Category: Guan, L.]]

[[Category: Iwata, S.]]

[[Category: Kaback, H.R.]]

[[Category: Kaback, H R.]]

[[Category: Mirza, O.]]

[[Category: Verner, G.]]

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[[Category: transport mechanism]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:06 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Cation-coupled active transport is an essential cellular process found, ubiquitously in all living organisms. Here, we present two novel, ligand-free X-ray structures of the lactose permease (LacY) of Escherichia, coli determined at acidic and neutral pH, and propose a model for the, mechanism of coupling between lactose and H+ translocation. No, sugar-binding site is observed in the absence of ligand, and deprotonation, of the key residue Glu269 is associated with ligand binding. Thus, substrate induces formation of the sugar-binding site, as well as the, initial step in H+ transduction.
+Cation-coupled active transport is an essential cellular process found ubiquitously in all living organisms. Here, we present two novel ligand-free X-ray structures of the lactose permease (LacY) of Escherichia coli determined at acidic and neutral pH, and propose a model for the mechanism of coupling between lactose and H+ translocation. No sugar-binding site is observed in the absence of ligand, and deprotonation of the key residue Glu269 is associated with ligand binding. Thus, substrate induces formation of the sugar-binding site, as well as the initial step in H+ transduction.
 ==About this Structure==
@@ Line 15: / Line 15: @@
 [[Category: Guan, L.]]
 [[Category: Iwata, S.]]
-[[Category: Kaback, H.R.]]
+[[Category: Kaback, H R.]]
 [[Category: Mirza, O.]]
 [[Category: Verner, G.]]
@@ Line 26: / Line 26: @@
 [[Category: transport mechanism]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:34:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:06 2008''