5ztf
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5ztf is ON HOLD Authors: Inoue, M., Watanabe, S., Inaba, K. Description: Ca2+ ATPase Category: Unreleased Structures Category: Inaba, K [[C...) |
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Structure of Ca2+ ATPase== |
| + | <StructureSection load='5ztf' size='340' side='right'caption='[[5ztf]], [[Resolution|resolution]] 3.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ztf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZTF 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]] 3.45Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5ztf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ztf OCA], [https://pdbe.org/5ztf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ztf RCSB], [https://www.ebi.ac.uk/pdbsum/5ztf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ztf ProSAT]</span></td></tr> | ||
| + | </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. | ||
| + | == Function == | ||
| + | [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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sarco/endoplasmic reticulum (ER) Ca(2+)-ATPase 2b (SERCA2b) is a ubiquitously expressed membrane protein that facilitates Ca(2+) uptake from the cytosol to the ER. SERCA2b includes a characteristic 11(th) transmembrane helix (TM11) followed by a luminal tail, but the structural basis of SERCA regulation by these C-terminal segments remains unclear. Here, we determined the crystal structures of SERCA2b and its C-terminal splicing variant SERCA2a, both in the E1-2Ca(2+)-adenylyl methylenediphosphonate (AMPPCP) state. Despite discrepancies with the previously reported structural model of SERCA2b, TM11 was found to be located adjacent to TM10 and to interact weakly with a part of the L8/9 loop and the N-terminal end of TM10, thereby inhibiting the SERCA2b catalytic cycle. Accordingly, mutational disruption of the interactions between TM11 and its neighboring residues caused SERCA2b to display SERCA2a-like ATPase activity. We propose that TM11 serves as a key modulator of SERCA2b activity by fine-tuning the intramolecular interactions with other transmembrane regions. | ||
| - | + | Structural Basis of Sarco/Endoplasmic Reticulum Ca(2+)-ATPase 2b Regulation via Transmembrane Helix Interplay.,Inoue M, Sakuta N, Watanabe S, Zhang Y, Yoshikaie K, Tanaka Y, Ushioda R, Kato Y, Takagi J, Tsukazaki T, Nagata K, Inaba K Cell Rep. 2019 Apr 23;27(4):1221-1230.e3. doi: 10.1016/j.celrep.2019.03.106. PMID:31018135<ref>PMID:31018135</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Inaba | + | <div class="pdbe-citations 5ztf" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: | + | ==See Also== |
| + | *[[ATPase 3D structures|ATPase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Inaba K]] | ||
| + | [[Category: Inoue M]] | ||
| + | [[Category: Watanabe S]] | ||
Current revision
Structure of Ca2+ ATPase
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