2fee: Difference between revisions

Revision as of 12:15, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2fee.png

Template:STRUCTURE 2fee

Structure of the Cl-/H+ exchanger CLC-ec1 from E.Coli in NaBrStructure of the Cl-/H+ exchanger CLC-ec1 from E.Coli in NaBr

Template:ABSTRACT PUBMED 16316975

About this StructureAbout this Structure

2FEE is a Single protein structure of sequence from Escherichia coli and Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Separate ion pathways in a Cl-/H+ exchanger., Accardi A, Walden M, Nguitragool W, Jayaram H, Williams C, Miller C, J Gen Physiol. 2005 Dec;126(6):563-70. PMID:16316975

Page seeded by OCA on Tue Jul 29 12:15:54 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2fee.gif|left|200px]]
+{{Seed}}
+[[Image:2fee.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2fee|  PDB=2fee  |  SCENE=  }}
-'''Structure of the Cl-/H+ exchanger CLC-ec1 from E.Coli in NaBr'''
+===Structure of the Cl-/H+ exchanger CLC-ec1 from E.Coli in NaBr===
-==Overview==
+<!--
-CLC-ec1 is a prokaryotic CLC-type Cl(-)/H+ exchange transporter. Little is known about the mechanism of H+ coupling to Cl-. A critical glutamate residue, E148, was previously shown to be required for Cl(-)/H+ exchange by mediating proton transfer between the protein and the extracellular solution. To test whether an analogous H+ acceptor exists near the intracellular side of the protein, we performed a mutagenesis scan of inward-facing carboxyl-bearing residues and identified E203 as the unique residue whose neutralization abolishes H+ coupling to Cl- transport. Glutamate at this position is strictly conserved in all known CLCs of the transporter subclass, while valine is always found here in CLC channels. The x-ray crystal structure of the E203Q mutant is similar to that of the wild-type protein. Cl- transport rate in E203Q is inhibited at neutral pH, and the double mutant, E148A/E203Q, shows maximal Cl- transport, independent of pH, as does the single mutant E148A. The results argue that substrate exchange by CLC-ec1 involves two separate but partially overlapping permeation pathways, one for Cl- and one for H+. These pathways are congruent from the protein's extracellular surface to E148, and they diverge beyond this point toward the intracellular side. This picture demands a transport mechanism fundamentally different from familiar alternating-access schemes.
+The line below this paragraph, {{ABSTRACT_PUBMED_16316975}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16316975 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16316975}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Clc-ec1]]
 [[Category: Clca_ecoli]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:47:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:15:54 2008''