2exw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:40, 23 August 2023) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2exw.gif|left|200px]]
 
-
{{Structure
+
==Crystal structure of a EcClC-Fab complex in the absence of bound ions==
-
|PDB= 2exw |SIZE=350|CAPTION= <scene name='initialview01'>2exw</scene>, resolution 3.20&Aring;
+
<StructureSection load='2exw' size='340' side='right'caption='[[2exw]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[2exw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EXW FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
-
|GENE=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2exw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2exw OCA], [https://pdbe.org/2exw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2exw RCSB], [https://www.ebi.ac.uk/pdbsum/2exw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2exw ProSAT]</span></td></tr>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=[[1ots|1OTS]], [[2exy|2EXY]], [[2ez0|2EZ0]]
+
== Function ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2exw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2exw OCA], [http://www.ebi.ac.uk/pdbsum/2exw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2exw RCSB]</span>
+
[https://www.uniprot.org/uniprot/CLCA_ECOLI CLCA_ECOLI] Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.<ref>PMID:12384697</ref> <ref>PMID:14985752</ref> <ref>PMID:16341087</ref> <ref>PMID:16905147</ref> <ref>PMID:18678918</ref>
-
}}
+
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ex/2exw_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2exw ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The ClC channels are members of a large protein family of chloride (Cl-) channels and secondary active Cl- transporters. Despite their diverse functions, the transmembrane architecture within the family is conserved. Here we present a crystallographic study on the ion-binding properties of the ClC selectivity filter in the close homolog from Escherichia coli (EcClC). The ClC selectivity filter contains three ion-binding sites that bridge the extra- and intracellular solutions. The sites bind Cl- ions with mM affinity. Despite their close proximity within the filter, the three sites can be occupied simultaneously. The ion-binding properties are found conserved from the bacterial transporter EcClC to the human Cl- channel ClC-1, suggesting a close functional link between ion permeation in the channels and active transport in the transporters. In resemblance to K+ channels, ions permeate the ClC channel in a single file, with mutual repulsion between the ions fostering rapid conduction.
-
'''Crystal structure of a EcClC-Fab complex in the absence of bound ions'''
+
Ion-binding properties of the ClC chloride selectivity filter.,Lobet S, Dutzler R EMBO J. 2006 Jan 11;25(1):24-33. Epub 2005 Dec 8. PMID:16341087<ref>PMID:16341087</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2exw" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
The ClC channels are members of a large protein family of chloride (Cl-) channels and secondary active Cl- transporters. Despite their diverse functions, the transmembrane architecture within the family is conserved. Here we present a crystallographic study on the ion-binding properties of the ClC selectivity filter in the close homolog from Escherichia coli (EcClC). The ClC selectivity filter contains three ion-binding sites that bridge the extra- and intracellular solutions. The sites bind Cl- ions with mM affinity. Despite their close proximity within the filter, the three sites can be occupied simultaneously. The ion-binding properties are found conserved from the bacterial transporter EcClC to the human Cl- channel ClC-1, suggesting a close functional link between ion permeation in the channels and active transport in the transporters. In resemblance to K+ channels, ions permeate the ClC channel in a single file, with mutual repulsion between the ions fostering rapid conduction.
+
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
2EXW is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EXW OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
Ion-binding properties of the ClC chloride selectivity filter., Lobet S, Dutzler R, EMBO J. 2006 Jan 11;25(1):24-33. Epub 2005 Dec 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16341087 16341087]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Single protein]]
+
[[Category: Dutzler R]]
-
[[Category: Dutzler, R.]]
+
[[Category: Lobet S]]
-
[[Category: Lobet, S.]]
+
-
[[Category: clc family of cl- channels and transporter]]
+
-
[[Category: h+/cl- antiporter]]
+
-
[[Category: membrane protein/fab complex]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:55:14 2008''
+

Current revision

Crystal structure of a EcClC-Fab complex in the absence of bound ions

PDB ID 2exw

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2exw"
Personal tools