1jvm

From Proteopedia

(Difference between revisions)

Revision as of 06:46, 11 August 2021

KCSA POTASSIUM CHANNEL WITH TBA (TETRABUTYLAMMONIUM) AND RUBIDIUM

Structural highlights

1jvm is a 4 chain structure with sequence from "actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1j95, 1bl8
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

The K+ selectivity filter catalyses the dehydration, transfer and rehydration of a K+ ion in about ten nanoseconds. This physical process is central to the production of electrical signals in biology. Here we show how nearly diffusion-limited rates are achieved, by analysing ion conduction and the corresponding crystallographic ion distribution in the selectivity filter of the KcsA K+ channel. Measurements with K+ and its slightly larger analogue, Rb+, lead us to conclude that the selectivity filter usually contains two K+ ions separated by one water molecule. The two ions move in a concerted fashion between two configurations, K+-water-K+-water (1,3 configuration) and water-K+-water-K+ (2,4 configuration), until a third ion enters, displacing the ion on the opposite side of the queue. For K+, the energy difference between the 1,3 and 2,4 configurations is close to zero, the condition of maximum conduction rate. The energetic balance between these configurations is a clear example of evolutionary optimization of protein function.

Energetic optimization of ion conduction rate by the K+ selectivity filter.,Morais-Cabral JH, Zhou Y, MacKinnon R Nature. 2001 Nov 1;414(6859):37-42. PMID:11689935^[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
↑ Morais-Cabral JH, Zhou Y, MacKinnon R. Energetic optimization of ion conduction rate by the K+ selectivity filter. Nature. 2001 Nov 1;414(6859):37-42. PMID:11689935 doi:http://dx.doi.org/10.1038/35102000

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/1jvm"

@@ Line 3: / Line 3: @@
 <StructureSection load='1jvm' size='340' side='right'caption='[[1jvm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jvm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JVM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1jvm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JVM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RB:RUBIDIUM+ION'>RB</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=RB:RUBIDIUM+ION'>RB</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">[[1j95|1j95]], [[1bl8|1bl8]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1j95|1j95]], [[1bl8|1bl8]]</div></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=1jvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvm OCA], [http://pdbe.org/1jvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jvm RCSB], [http://www.ebi.ac.uk/pdbsum/1jvm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jvm ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvm OCA], [https://pdbe.org/1jvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jvm RCSB], [https://www.ebi.ac.uk/pdbsum/1jvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jvm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KCSA_STRLI 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(+).<ref>PMID:7489706</ref>
+[[https://www.uniprot.org/uniprot/KCSA_STRLI 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(+).<ref>PMID:7489706</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Potassium Channel|Potassium Channel]]
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
 == References ==
 <references/>

1jvm

From Proteopedia

Revision as of 06:46, 11 August 2021

KCSA POTASSIUM CHANNEL WITH TBA (TETRABUTYLAMMONIUM) AND RUBIDIUM

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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