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.

2jk5

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:53, 15 April 2020

Potassium Channel KcsA in complex with Tetrabutylammonium in high K

Structural highlights

2jk5 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, 2w0f, 2ih1, 1j95, 2h8p, 1r3l, 2atk, 4uuj
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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/2jk5"

@@ Line 1: / Line 1: @@
 ==Potassium Channel KcsA in complex with Tetrabutylammonium in high K==
-<StructureSection load='2jk5' size='340' side='right' caption='[[2jk5]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='2jk5' size='340' side='right'caption='[[2jk5]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2jk5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JK5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JK5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2jk5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JK5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2JK5 FirstGlance]. <br>
-</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=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=HP6:HEPTANE'>HP6</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=L2C:(2S)-3-HYDROXY-2-(NONANOYLOXY)PROPYL+LAURATE'>L2C</scene>, <scene name='pdbligand=TBA:TETRABUTYLAMMONIUM+ION'>TBA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=HP6:HEPTANE'>HP6</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=L2C:(2S)-3-HYDROXY-2-(NONANOYLOXY)PROPYL+LAURATE'>L2C</scene>, <scene name='pdbligand=TBA:TETRABUTYLAMMONIUM+ION'>TBA</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]], [[2w0f|2w0f]], [[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=2jk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jk5 OCA], [http://pdbe.org/2jk5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jk5 RCSB], [http://www.ebi.ac.uk/pdbsum/2jk5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jk5 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2jk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jk5 OCA], [http://pdbe.org/2jk5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jk5 RCSB], [http://www.ebi.ac.uk/pdbsum/2jk5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jk5 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 32: / Line 32: @@
 ==See Also==
 *[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
-*[[Potassium Channel|Potassium Channel]]
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
 == References ==
 <references/>
@@ Line 38: / Line 38: @@
 </StructureSection>
 [[Category: Actinomyces lividans krasil'nikov et al. 1965]]
+[[Category: Large Structures]]
 [[Category: Lk3 transgenic mice]]
 [[Category: Focia, P J]]

2jk5

From Proteopedia

Revision as of 07:53, 15 April 2020

Potassium Channel KcsA in complex with Tetrabutylammonium in high K

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox