This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2cfq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 8: Line 8:
==About this Structure==
==About this Structure==
-
2CFQ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with HG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CFQ OCA]].
+
2CFQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with HG as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CFQ OCA].
==Reference==
==Reference==
Line 27: Line 27:
[[Category: transport mechanism]]
[[Category: transport mechanism]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:06:59 2007''
+
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:38:45 2007''

Revision as of 10:33, 5 November 2007


2cfq, resolution 2.95Å

Drag the structure with the mouse to rotate

SUGAR FREE LACTOSE PERMEASE AT NEUTRAL 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.

About this Structure

2CFQ is a Single protein structure of sequence from Escherichia coli with HG as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY., Mirza O, Guan L, Verner G, Iwata S, Kaback HR, EMBO J. 2006 Mar 22;25(6):1177-83. Epub 2006 Mar 9. PMID:16525509

Page seeded by OCA on Mon Nov 5 12:38:45 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools