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7x20

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Crystal structure of non gastric H,K-ATPase alpha2 in (K+)E2-AlF state

Structural highlights

7x20 is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.3Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AT12A_RAT The catalytic subunit of a H(+)/K(+) ATPase and/or Na(+)/K(+) ATPase pump which transports K(+) ions in exchange for Na(+) and/or H(+) ions across the apical membrane of epithelial cells. Uses ATP as an energy source to pump K(+) ions into the cell while transporting Na(+) and/or H(+) ions to the extracellular compartment (PubMed:10644526, PubMed:7560093). Involved in the maintenance of electrolyte homeostasis through K(+) ion absorption in kidney and colon (By similarity). In the airway epithelium, may play a primary role in mucus acidification regulating its viscosity and clearance (By similarity).[UniProtKB:P54707][UniProtKB:Q9Z1W8]^[1] ^[2]

Publication Abstract from PubMed

Ion-transport mechanisms evolve by changing ion-selectivity, such as switching from Na(+) to H(+) selectivity in secondary-active transporters or P-type-ATPases. Here we study primary-active transport via P-type ATPases using functional and structural analyses to demonstrate that four simultaneous residue substitutions transform the non-gastric H(+)/K(+) pump, a strict H(+)-dependent electroneutral P-type ATPase, into a bona fide Na(+)-dependent electrogenic Na(+)/K(+) pump. Conversion of a H(+)-dependent primary-active transporter into a Na(+)-dependent one provides a prototype for similar studies of ion-transport proteins. Moreover, we solve the structures of the wild-type non-gastric H(+)/K(+) pump, a suitable drug target to treat cystic fibrosis, and of its Na(+)/K(+) pump-mimicking mutant in two major conformations, providing insight on how Na(+) binding drives a concerted mechanism leading to Na(+)/K(+) pump phosphorylation.

Structure and function of H(+)/K(+) pump mutants reveal Na(+)/K(+) pump mechanisms.,Young VC, Nakanishi H, Meyer DJ, Nishizawa T, Oshima A, Artigas P, Abe K Nat Commun. 2022 Sep 9;13(1):5270. doi: 10.1038/s41467-022-32793-0. PMID:36085139^[3]

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

References

↑ Sangan P, Thevananther S, Sangan S, Rajendran VM, Binder HJ. Colonic H-K-ATPase alpha- and beta-subunits express ouabain-insensitive H-K-ATPase. Am J Physiol Cell Physiol. 2000 Jan;278(1):C182-9. doi:, 10.1152/ajpcell.2000.278.1.C182. PMID:10644526 doi:http://dx.doi.org/10.1152/ajpcell.2000.278.1.C182
↑ Lee J, Rajendran VM, Mann AS, Kashgarian M, Binder HJ. Functional expression and segmental localization of rat colonic K-adenosine triphosphatase. J Clin Invest. 1995 Oct;96(4):2002-8. doi: 10.1172/JCI118247. PMID:7560093 doi:http://dx.doi.org/10.1172/JCI118247
↑ Young VC, Nakanishi H, Meyer DJ, Nishizawa T, Oshima A, Artigas P, Abe K. Structure and function of H(+)/K(+) pump mutants reveal Na(+)/K(+) pump mechanisms. Nat Commun. 2022 Sep 9;13(1):5270. doi: 10.1038/s41467-022-32793-0. PMID:36085139 doi:http://dx.doi.org/10.1038/s41467-022-32793-0

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/7x20"

Categories: Large Structures | Rattus norvegicus | Abe K | Nakanishi H

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7x20 is ON HOLD
+==Crystal structure of non gastric H,K-ATPase alpha2 in (K+)E2-AlF state==
+<StructureSection load='7x20' size='340' side='right'caption='[[7x20]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7x20]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7X20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7X20 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=7x20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7x20 OCA], [https://pdbe.org/7x20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7x20 RCSB], [https://www.ebi.ac.uk/pdbsum/7x20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7x20 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AT12A_RAT AT12A_RAT] The catalytic subunit of a H(+)/K(+) ATPase and/or Na(+)/K(+) ATPase pump which transports K(+) ions in exchange for Na(+) and/or H(+) ions across the apical membrane of epithelial cells. Uses ATP as an energy source to pump K(+) ions into the cell while transporting Na(+) and/or H(+) ions to the extracellular compartment (PubMed:10644526, PubMed:7560093). Involved in the maintenance of electrolyte homeostasis through K(+) ion absorption in kidney and colon (By similarity). In the airway epithelium, may play a primary role in mucus acidification regulating its viscosity and clearance (By similarity).[UniProtKB:P54707][UniProtKB:Q9Z1W8]<ref>PMID:10644526</ref> <ref>PMID:7560093</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Ion-transport mechanisms evolve by changing ion-selectivity, such as switching from Na(+) to H(+) selectivity in secondary-active transporters or P-type-ATPases. Here we study primary-active transport via P-type ATPases using functional and structural analyses to demonstrate that four simultaneous residue substitutions transform the non-gastric H(+)/K(+) pump, a strict H(+)-dependent electroneutral P-type ATPase, into a bona fide Na(+)-dependent electrogenic Na(+)/K(+) pump. Conversion of a H(+)-dependent primary-active transporter into a Na(+)-dependent one provides a prototype for similar studies of ion-transport proteins. Moreover, we solve the structures of the wild-type non-gastric H(+)/K(+) pump, a suitable drug target to treat cystic fibrosis, and of its Na(+)/K(+) pump-mimicking mutant in two major conformations, providing insight on how Na(+) binding drives a concerted mechanism leading to Na(+)/K(+) pump phosphorylation.
-Authors:
+Structure and function of H(+)/K(+) pump mutants reveal Na(+)/K(+) pump mechanisms.,Young VC, Nakanishi H, Meyer DJ, Nishizawa T, Oshima A, Artigas P, Abe K Nat Commun. 2022 Sep 9;13(1):5270. doi: 10.1038/s41467-022-32793-0. PMID:36085139<ref>PMID:36085139</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7x20" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ATPase 3D structures|ATPase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Rattus norvegicus]]
+[[Category: Abe K]]
+[[Category: Nakanishi H]]

7x20

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Current revision

Crystal structure of non gastric H,K-ATPase alpha2 in (K+)E2-AlF state

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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