7x20: Difference between revisions
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==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]] 3.30Å' 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]] 3.3Å</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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </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]] | |||
Latest revision as of 20:46, 29 November 2023
Crystal structure of non gastric H,K-ATPase alpha2 in (K+)E2-AlF stateCrystal structure of non gastric H,K-ATPase alpha2 in (K+)E2-AlF state
Structural highlights
FunctionAT12A_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 PubMedIon-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. See AlsoReferences
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