7n9k: Difference between revisions

Latest revision as of 16:26, 18 October 2023

KirBac3.1 L124M mutant

Structural highlights

7n9k is a 1 chain structure with sequence from Magnetospirillum magnetotacticum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.72Å
Ligands:	K, OCT, PCW, TMO
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IRK10_MAGMG Inward rectifier potassium channel that mediates potassium uptake into the cell. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. The inward rectification may be achieved by the blockage of outward current by cytoplasmic divalent metal ions and polyamines. Complements an E.coli mutant that is defective in K(+) uptake.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Ion currents through potassium channels are gated. Constriction of the ion conduction pathway at the inner helix bundle, the textbook gate of Kir potassium channels, has been shown to be an ineffective permeation control, creating a rift in our understanding of how these channels are gated. Here we present evidence that anionic lipids act as interactive response elements sufficient to gate potassium conduction. We demonstrate the limiting barrier to K(+) permeation lies within the ion conduction pathway and show that this gate is operated by the fatty acyl tails of lipids that infiltrate the conduction pathway via fenestrations in the walls of the pore. Acyl tails occupying a surface groove extending from the cytosolic interface to the conduction pathway provide a potential means of relaying cellular signals, mediated by anionic lipid head groups bound at the canonical lipid binding site, to the internal gate.

Ion currents through Kir potassium channels are gated by anionic lipids.,Jin R, He S, Black KA, Clarke OB, Wu D, Bolla JR, Johnson P, Periasamy A, Wardak A, Czabotar P, Colman PM, Robinson CV, Laver D, Smith BJ, Gulbis JM Nat Commun. 2022 Jan 25;13(1):490. doi: 10.1038/s41467-022-28148-4. PMID:35079013^[4]

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

References

↑ Paynter JJ, Andres-Enguix I, Fowler PW, Tottey S, Cheng W, Enkvetchakul D, Bavro VN, Kusakabe Y, Sansom MS, Robinson NJ, Nichols CG, Tucker SJ. Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains. J Biol Chem. 2010 Dec 24;285(52):40754-61. doi: 10.1074/jbc.M110.175687. Epub, 2010 Sep 28. PMID:20876570 doi:https://dx.doi.org/10.1074/jbc.M110.175687
↑ Clarke OB, Caputo AT, Hill AP, Vandenberg JI, Smith BJ, Gulbis JM. Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels. Cell. 2010 Jun 11;141(6):1018-29. PMID:20564790
↑ Bavro VN, De Zorzi R, Schmidt MR, Muniz JR, Zubcevic L, Sansom MS, Venien-Bryan C, Tucker SJ. Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating. Nat Struct Mol Biol. 2012 Jan 8;19(2):158-63. doi: 10.1038/nsmb.2208. PMID:22231399 doi:10.1038/nsmb.2208
↑ Jin R, He S, Black KA, Clarke OB, Wu D, Bolla JR, Johnson P, Periasamy A, Wardak A, Czabotar P, Colman PM, Robinson CV, Laver D, Smith BJ, Gulbis JM. Ion currents through Kir potassium channels are gated by anionic lipids. Nat Commun. 2022 Jan 25;13(1):490. doi: 10.1038/s41467-022-28148-4. PMID:35079013 doi:https://dx.doi.org/10.1038/s41467-022-28148-4

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Paynter JJ, Andres-Enguix I, Fowler PW, Tottey S, Cheng W, Enkvetchakul D, Bavro VN, Kusakabe Y, Sansom MS, Robinson NJ, Nichols CG, Tucker SJ. Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains. J Biol Chem. 2010 Dec 24;285(52):40754-61. doi: 10.1074/jbc.M110.175687. Epub, 2010 Sep 28. PMID:20876570 doi:https://dx.doi.org/10.1074/jbc.M110.175687

[2] Clarke OB, Caputo AT, Hill AP, Vandenberg JI, Smith BJ, Gulbis JM. Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels. Cell. 2010 Jun 11;141(6):1018-29. PMID:20564790

[3] Bavro VN, De Zorzi R, Schmidt MR, Muniz JR, Zubcevic L, Sansom MS, Venien-Bryan C, Tucker SJ. Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating. Nat Struct Mol Biol. 2012 Jan 8;19(2):158-63. doi: 10.1038/nsmb.2208. PMID:22231399 doi:10.1038/nsmb.2208

[4] Jin R, He S, Black KA, Clarke OB, Wu D, Bolla JR, Johnson P, Periasamy A, Wardak A, Czabotar P, Colman PM, Robinson CV, Laver D, Smith BJ, Gulbis JM. Ion currents through Kir potassium channels are gated by anionic lipids. Nat Commun. 2022 Jan 25;13(1):490. doi: 10.1038/s41467-022-28148-4. PMID:35079013 doi:https://dx.doi.org/10.1038/s41467-022-28148-4

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@@ Line 3: / Line 3: @@
 <StructureSection load='7n9k' size='340' side='right'caption='[[7n9k]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7n9k]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N9K FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7n9k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Magnetospirillum_magnetotacticum Magnetospirillum magnetotacticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N9K FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</scene>, <scene name='pdbligand=TMO:TRIMETHYLAMINE+OXIDE'>TMO</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.72&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</scene>, <scene name='pdbligand=TMO:TRIMETHYLAMINE+OXIDE'>TMO</scene></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=7n9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n9k OCA], [https://pdbe.org/7n9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n9k RCSB], [https://www.ebi.ac.uk/pdbsum/7n9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n9k ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/IRK10_MAGMG IRK10_MAGMG]] Inward rectifier potassium channel that mediates potassium uptake into the cell. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. The inward rectification may be achieved by the blockage of outward current by cytoplasmic divalent metal ions and polyamines. Complements an E.coli mutant that is defective in K(+) uptake.<ref>PMID:20876570</ref> <ref>PMID:20564790</ref> <ref>PMID:22231399</ref>
+[https://www.uniprot.org/uniprot/IRK10_MAGMG IRK10_MAGMG] Inward rectifier potassium channel that mediates potassium uptake into the cell. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. The inward rectification may be achieved by the blockage of outward current by cytoplasmic divalent metal ions and polyamines. Complements an E.coli mutant that is defective in K(+) uptake.<ref>PMID:20876570</ref> <ref>PMID:20564790</ref> <ref>PMID:22231399</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 26: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Black, T A]]
+[[Category: Magnetospirillum magnetotacticum]]
-[[Category: Gulbis, J M]]
+[[Category: Black TA]]
-[[Category: Membrane protein]]
+[[Category: Gulbis JM]]
-[[Category: Mutant]]
-[[Category: Potassium channel gating]]

7n9k: Difference between revisions

Latest revision as of 16:26, 18 October 2023

KirBac3.1 L124M mutant

Structural highlights

Function

Publication Abstract from PubMed

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References

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