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2w0f

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Revision as of 07:40, 7 February 2016

Potassium Channel KcsA-Fab Complex with Tetraoctylammonium

Structural highlights

2w0f is a 3 chain structure with sequence from "actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965 and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	1r3k, 2a9h, 1k4d, 1k4c, 2hg5, 2bob, 1f6g, 2boc, 1jq2, 1r3j, 1jvm, 1jq1, 2ih3, 1zwi, 1bl8, 1r3i, 2ih1, 1j95, 2h8p, 1r3l, 2atk, 4uuj
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[KCSA_STRLI] Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Potassium channels allow for the passive movement of potassium ions across the cell membrane and are instrumental in controlling the membrane potential in all cell types. Quaternary ammonium (QA) compounds block potassium channels and have long been used to study the functional and structural properties of these channels. Here we describe the interaction between three symmetrical hydrophobic QAs and the prokaryotic potassium channel KcsA. The structures demonstrate the presence of a hydrophobic pocket between the inner helices of KcsA and provide insight into the binding site and blocking mechanism of hydrophobic QAs. The structures also reveal a structurally hidden pathway between the central cavity and the outside membrane environment reminiscent of the lateral fenestration observed in sodium channels that can be accessed through small conformational changes in the pore wall. We propose that the hydrophobic binding pocket stabilizes the alkyl chains of long-chain QA molecules and may play a key role in hydrophobic drug binding in general.

Structures of KcsA in Complex with Symmetrical Quaternary Ammonium Compounds Reveal a Hydrophobic Binding Site.,Lenaeus MJ, Burdette D, Wagner T, Focia PJ, Gross A Biochemistry. 2014 Aug 19;53(32):5365-73. doi: 10.1021/bi500525s. Epub 2014 Aug, 8. PMID:25093676^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schrempf H, Schmidt O, Kummerlen R, Hinnah S, Muller D, Betzler M, Steinkamp T, Wagner R. A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 1995 Nov 1;14(21):5170-8. PMID:7489706
↑ Lenaeus MJ, Burdette D, Wagner T, Focia PJ, Gross A. Structures of KcsA in Complex with Symmetrical Quaternary Ammonium Compounds Reveal a Hydrophobic Binding Site. Biochemistry. 2014 Aug 19;53(32):5365-73. doi: 10.1021/bi500525s. Epub 2014 Aug, 8. PMID:25093676 doi:http://dx.doi.org/10.1021/bi500525s

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2w0f"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=DGA:DIACYL+GLYCEROL'>DGA</scene>, <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=HX0:N,N,N-TRIOCTYLOCTAN-1-AMINIUM'>HX0</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r3k|1r3k]], [[2a9h|2a9h]], [[1k4d|1k4d]], [[1k4c|1k4c]], [[2hg5|2hg5]], [[2bob|2bob]], [[1f6g|1f6g]], [[2boc|2boc]], [[1jq2|1jq2]], [[1r3j|1r3j]], [[1jvm|1jvm]], [[1jq1|1jq1]], [[2ih3|2ih3]], [[1zwi|1zwi]], [[1bl8|1bl8]], [[1r3i|1r3i]], [[2ih1|2ih1]], [[1j95|1j95]], [[2h8p|2h8p]], [[1r3l|1r3l]], [[2atk|2atk]], [[4uuj|4uuj]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w0f RCSB], [http://www.ebi.ac.uk/pdbsum/2w0f PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w0f OCA], [http://pdbe.org/2w0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w0f RCSB], [http://www.ebi.ac.uk/pdbsum/2w0f PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 17: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2w0f ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2w0f" style="background-color:#fffaf0;"></div>
 ==See Also==

2w0f

From Proteopedia

Revision as of 07:40, 7 February 2016

Potassium Channel KcsA-Fab Complex with Tetraoctylammonium

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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