2h2p: Difference between revisions

Line 1:

[[Image:2h2p.gif|left|200px]]<br /><applet load="2h2p" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2h2p.gif|left|200px]]<br /><applet load="2h2p" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2h2p, resolution 3.100Å" />

'''Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-'''<br />

==Overview==

CLC-ec1 is a bacterial archetype of CLC transporters, a ubiquitous class, of proteins that catalyze transmembrane exchange of Cl- and H+ necessary, for pH regulation of numerous physiological processes. Despite a profusion, of high-resolution structures, the molecular mechanism of exchange remains, unknown. Here, we rigorously demonstrate strict exchange stoichiometry of, 2 Cl-/1 H+. In addition to Cl- and Br-, two non-halide ions, NO3- and, SCN-, are shown to be transported by CLC-ec1, but with reduced H+, counter-transport. The loss of proton coupling to these anions is, accompanied by an absence of bound anions in the central and external Cl-, binding sites in the protein's anion selectivity region, as revealed by, crystallographic comparison of Br- and SeCN- bound to this region.

CLC-ec1 is a bacterial archetype of CLC transporters, a ubiquitous class of proteins that catalyze transmembrane exchange of Cl- and H+ necessary for pH regulation of numerous physiological processes. Despite a profusion of high-resolution structures, the molecular mechanism of exchange remains unknown. Here, we rigorously demonstrate strict exchange stoichiometry of 2 Cl-/1 H+. In addition to Cl- and Br-, two non-halide ions, NO3- and SCN-, are shown to be transported by CLC-ec1, but with reduced H+ counter-transport. The loss of proton coupling to these anions is accompanied by an absence of bound anions in the central and external Cl- binding sites in the protein's anion selectivity region, as revealed by crystallographic comparison of Br- and SeCN- bound to this region.

==About this Structure==

2H2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SEK as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2H2P OCA].

2H2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SEK:'>SEK</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2P OCA].

==Reference==

Line 19:

[[Category: clc; transporter; chloride; antiport]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 11:31:~~11 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:36 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2h2p.gif|left|200px]]<br /><applet load="2h2p" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2h2p.gif|left|200px]]<br /><applet load="2h2p" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2h2p, resolution 3.100&Aring;" />
 '''Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-'''<br />
 ==Overview==
-CLC-ec1 is a bacterial archetype of CLC transporters, a ubiquitous class, of proteins that catalyze transmembrane exchange of Cl- and H+ necessary, for pH regulation of numerous physiological processes. Despite a profusion, of high-resolution structures, the molecular mechanism of exchange remains, unknown. Here, we rigorously demonstrate strict exchange stoichiometry of, 2 Cl-/1 H+. In addition to Cl- and Br-, two non-halide ions, NO3- and, SCN-, are shown to be transported by CLC-ec1, but with reduced H+, counter-transport. The loss of proton coupling to these anions is, accompanied by an absence of bound anions in the central and external Cl-, binding sites in the protein's anion selectivity region, as revealed by, crystallographic comparison of Br- and SeCN- bound to this region.
+CLC-ec1 is a bacterial archetype of CLC transporters, a ubiquitous class of proteins that catalyze transmembrane exchange of Cl- and H+ necessary for pH regulation of numerous physiological processes. Despite a profusion of high-resolution structures, the molecular mechanism of exchange remains unknown. Here, we rigorously demonstrate strict exchange stoichiometry of 2 Cl-/1 H+. In addition to Cl- and Br-, two non-halide ions, NO3- and SCN-, are shown to be transported by CLC-ec1, but with reduced H+ counter-transport. The loss of proton coupling to these anions is accompanied by an absence of bound anions in the central and external Cl- binding sites in the protein's anion selectivity region, as revealed by crystallographic comparison of Br- and SeCN- bound to this region.
 ==About this Structure==
-H2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SEK as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H2P OCA].
+H2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SEK:'>SEK</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2P OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: clc; transporter; chloride; antiport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:31:11 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:36 2008''