2cfp: Difference between revisions

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[[Image:2cfp.~~gif~~|left|200px]]

[[Image:2cfp.png|left|200px]]

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~~'''~~SUGAR FREE LACTOSE PERMEASE AT ACIDIC PH~~'''~~

===SUGAR FREE LACTOSE PERMEASE AT ACIDIC PH===

~~==Overview==~~

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~~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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_16525509}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16525509 is the PubMed ID number.

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==About this Structure==

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[[Category: Transmembrane]]

[[Category: Transport mechanism]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 22~~:01:44 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:53:45 2008''

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-[[Image:2cfp.gif|left|200px]]
+{{Seed}}
+[[Image:2cfp.png|left|200px]]
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 {{STRUCTURE_2cfp|  PDB=2cfp  |  SCENE=  }}
-'''SUGAR FREE LACTOSE PERMEASE AT ACIDIC PH'''
+===SUGAR FREE LACTOSE PERMEASE AT ACIDIC PH===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16525509}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16525509 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16525509}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Transmembrane]]
 [[Category: Transport mechanism]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 22:01:44 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:53:45 2008''