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| | <StructureSection load='6jxk' size='340' side='right'caption='[[6jxk]], [[Resolution|resolution]] 4.30Å' scene=''> | | <StructureSection load='6jxk' size='340' side='right'caption='[[6jxk]], [[Resolution|resolution]] 4.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jxk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JXK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JXK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jxk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JXK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MF4:TETRAFLUOROMAGNESATE(2-)'>MF4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 4.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATP4A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG]), ATP4B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MF4:TETRAFLUOROMAGNESATE(2-)'>MF4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)/K(+)-exchanging_ATPase H(+)/K(+)-exchanging ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=7.2.2.19 7.2.2.19] </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=6jxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jxk OCA], [https://pdbe.org/6jxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jxk RCSB], [https://www.ebi.ac.uk/pdbsum/6jxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jxk ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jxk OCA], [http://pdbe.org/6jxk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jxk RCSB], [http://www.ebi.ac.uk/pdbsum/6jxk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jxk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | == Disease == | |
| - | [[http://www.uniprot.org/uniprot/ATP4B_PIG ATP4B_PIG]] Note=Parietal cell autoantigen associated with autoimmune gastritis. | |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ATP4A_PIG ATP4A_PIG]] Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for acid production in the stomach. | + | [https://www.uniprot.org/uniprot/ATP4A_PIG ATP4A_PIG] Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for acid production in the stomach. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pig]] | + | [[Category: Sus scrofa]] |
| - | [[Category: Abe, K]] | + | [[Category: Abe K]] |
| - | [[Category: Irie, K]] | + | [[Category: Irie K]] |
| - | [[Category: Yamamoto, K]] | + | [[Category: Yamamoto K]] |
| - | [[Category: Gastric]]
| + | |
| - | [[Category: Ion pump]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: P-type atpase]]
| + | |
| - | [[Category: Proton pump]]
| + | |
| Structural highlights
6jxk is a 4 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 4.3Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
ATP4A_PIG Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for acid production in the stomach.
Publication Abstract from PubMed
The gastric proton pump (H(+),K(+)-ATPase), a P-type ATPase responsible for gastric acidification, mediates electro-neutral exchange of H(+) and K(+) coupled with ATP hydrolysis, but with an as yet undetermined transport stoichiometry. Here we show crystal structures at a resolution of 2.5 A of the pump in the E2-P transition state, in which the counter-transporting cation is occluded. We found a single K(+) bound to the cation-binding site of the H(+),K(+)-ATPase, indicating an exchange of 1H(+)/1K(+) per hydrolysis of one ATP molecule. This fulfills the energy requirement for the generation of a six pH unit gradient across the membrane. The structural basis of K(+) recognition is resolved and supported by molecular dynamics simulations, establishing how the H(+),K(+)-ATPase overcomes the energetic challenge to generate an H(+) gradient of more than a million-fold-one of the highest cation gradients known in mammalian tissue-across the membrane.
A single K(+)-binding site in the crystal structure of the gastric proton pump.,Yamamoto K, Dubey V, Irie K, Nakanishi H, Khandelia H, Fujiyoshi Y, Abe K Elife. 2019 Aug 22;8. pii: 47701. doi: 10.7554/eLife.47701. PMID:31436534[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yamamoto K, Dubey V, Irie K, Nakanishi H, Khandelia H, Fujiyoshi Y, Abe K. A single K(+)-binding site in the crystal structure of the gastric proton pump. Elife. 2019 Aug 22;8. pii: 47701. doi: 10.7554/eLife.47701. PMID:31436534 doi:http://dx.doi.org/10.7554/eLife.47701
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