7adi

From Proteopedia

(Difference between revisions)

Current revision

KirBac3.1 W46R: role of a highly conserved tryptophan at the membrane-water interface of Kir channel

Structural highlights

7adi is a 2 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 2.8Å
Ligands:	,
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

ATP-sensitive potassium (K-ATP) channels are ubiquitously expressed on the plasma membrane of cells in several organs, including the heart, pancreas, and brain, and they govern a wide range of physiological processes. In pancreatic beta-cells, K-ATP channels composed of Kir6.2 and SUR1 play a key role in coupling blood glucose and insulin secretion. A tryptophan residue located at the cytosolic end of the transmembrane helix is highly conserved in eukaryote and prokaryote Kir channels. Any mutation on this amino acid causes a gain of function and neonatal diabetes mellitus. In this study, we have investigated the effect of mutation on this highly conserved residue on a KirBac channel (prokaryotic homolog of mammalian Kir6.2). We provide the crystal structure of the mutant KirBac3.1 W46R (equivalent to W68R in Kir6.2) and its conformational flexibility properties using HDX-MS. In addition, the detailed dynamical view of the mutant during the gating was investigated using the in silico method. Finally, functional assays have been performed. A comparison of important structural determinants for the gating mechanism between the wild type KirBac and the mutant W46R suggests interesting structural and dynamical clues and a mechanism of action of the mutation that leads to the gain of function.

Integrative Study of the Structural and Dynamical Properties of a KirBac3.1 Mutant: Functional Implication of a Highly Conserved Tryptophan in the Transmembrane Domain.,Fagnen C, Bannwarth L, Oubella I, Zuniga D, Haouz A, Forest E, Scala R, Bendahhou S, De Zorzi R, Perahia D, Venien-Bryan C Int J Mol Sci. 2021 Dec 29;23(1). pii: ijms23010335. doi: 10.3390/ijms23010335. PMID:35008764^[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:http://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
↑ Fagnen C, Bannwarth L, Oubella I, Zuniga D, Haouz A, Forest E, Scala R, Bendahhou S, De Zorzi R, Perahia D, Venien-Bryan C. Integrative Study of the Structural and Dynamical Properties of a KirBac3.1 Mutant: Functional Implication of a Highly Conserved Tryptophan in the Transmembrane Domain. Int J Mol Sci. 2021 Dec 29;23(1). pii: ijms23010335. doi: 10.3390/ijms23010335. PMID:35008764 doi:http://dx.doi.org/10.3390/ijms23010335

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7adi"

@@ Line 3: / Line 3: @@
 <StructureSection load='7adi' size='340' side='right'caption='[[7adi]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7adi]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ADI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ADI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7adi]] is a 2 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=7ADI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ADI 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=MG:MAGNESIUM+ION'>MG</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]] 2.8&#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=MG:MAGNESIUM+ION'>MG</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=7adi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7adi OCA], [https://pdbe.org/7adi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7adi RCSB], [https://www.ebi.ac.uk/pdbsum/7adi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7adi 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 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 7adi" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
 == References ==
 <references/>
@@ Line 23: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Bannwarth, L]]
+[[Category: Magnetospirillum magnetotacticum]]
-[[Category: Fagnen, C]]
+[[Category: Bannwarth L]]
-[[Category: Haouz, A]]
+[[Category: De Zorzi R]]
-[[Category: Oubella, I]]
+[[Category: Fagnen C]]
-[[Category: Venien-Bryan, C]]
+[[Category: Haouz A]]
-[[Category: Zorzi, R De]]
+[[Category: Oubella I]]
-[[Category: Inward rectifier]]
+[[Category: Venien-Bryan C]]
-[[Category: Ion channel]]
-[[Category: Membrane protein]]
-[[Category: Metal transport]]
-[[Category: Potassium channel]]

7adi

From Proteopedia

Current revision

KirBac3.1 W46R: role of a highly conserved tryptophan at the membrane-water interface of Kir channel

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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