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| <StructureSection load='7e7s' size='340' side='right'caption='[[7e7s]], [[Resolution|resolution]] 3.30Å' scene=''> | | <StructureSection load='7e7s' size='340' side='right'caption='[[7e7s]], [[Resolution|resolution]] 3.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7e7s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E7S FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E7S FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATP2A2, ATP2B ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/P-type_Ca(2+)_transporter P-type Ca(2+) transporter], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=7.2.2.10 7.2.2.10] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7e7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e7s OCA], [https://pdbe.org/7e7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e7s RCSB], [https://www.ebi.ac.uk/pdbsum/7e7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e7s ProSAT]</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=7e7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e7s OCA], [https://pdbe.org/7e7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e7s RCSB], [https://www.ebi.ac.uk/pdbsum/7e7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e7s ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Disease ==
| |
| [[https://www.uniprot.org/uniprot/AT2A2_HUMAN AT2A2_HUMAN]] Darier disease;Acrokeratosis verruciformis of Hopf. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
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| == Function ==
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| [[https://www.uniprot.org/uniprot/AT2A2_HUMAN AT2A2_HUMAN]] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the regulation of the contraction/relaxation cycle (PubMed:16402920). Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca (2+) signaling cascades that promote osteoclast differentiation and activation (By similarity).[UniProtKB:O55143]<ref>PMID:16402920</ref>
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Sarco/endoplasmic reticulum Ca(2+) -ATPase (SERCA) 2b is a ubiquitous SERCA family member that conducts Ca(2+) uptake from the cytosol to the ER. Herein, we present a 3.3 A resolution cryo-electron microscopy (cryo-EM) structure of human SERCA2b in the E1.2Ca(2+) state, revealing a new conformation for Ca(2+) -bound SERCA2b with a much closer arrangement of cytosolic domains than in the previously reported crystal structure of Ca(2+) -bound SERCA1a. Multiple conformations generated by 3D classification of cryo-EM maps reflect the intrinsically dynamic nature of the cytosolic domains in this state. Notably, ATP binding residues of SERCA2b in the E1.2Ca(2+) state are located at similar positions to those in the E1.2Ca(2+) -ATP state; hence, the cryo-EM structure likely represents a preformed state immediately prior to ATP binding. Consistently, a SERCA2b mutant with an interdomain disulfide bridge that locks the closed cytosolic domain arrangement displayed significant autophosphorylation activity in the presence of Ca(2+) . We propose a novel mechanism of ATP binding to SERCA2b.
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| Cryo-EM analysis provides new mechanistic insight into ATP binding to Ca(2+) -ATPase SERCA2b.,Zhang Y, Watanabe S, Tsutsumi A, Kadokura H, Kikkawa M, Inaba K EMBO J. 2021 Oct 1;40(19):e108482. doi: 10.15252/embj.2021108482. Epub 2021 Aug, 30. PMID:34459010<ref>PMID:34459010</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7e7s" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Inaba, K]] | | [[Category: Inaba K]] |
| [[Category: Tsutsumi, A]] | | [[Category: Tsutsumi A]] |
| [[Category: Watanabe, S]] | | [[Category: Watanabe S]] |
| [[Category: Zhang, Y]] | | [[Category: Zhang Y]] |
| [[Category: Calcium]]
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| [[Category: Metal transport]]
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