7bt2
From Proteopedia
(Difference between revisions)
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==Crystal structure of the SERCA2a in the E2.ATP state== | ==Crystal structure of the SERCA2a in the E2.ATP state== | ||
| - | <StructureSection load='7bt2' size='340' side='right'caption='[[7bt2]]' scene=''> | + | <StructureSection load='7bt2' size='340' side='right'caption='[[7bt2]], [[Resolution|resolution]] 3.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BT2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7BT2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7bt2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BT2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7BT2 FirstGlance]. <br> |
| - | </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=7bt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bt2 OCA], [http://pdbe.org/7bt2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7bt2 RCSB], [http://www.ebi.ac.uk/pdbsum/7bt2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7bt2 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATP2A2, ATP2B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/P-type_Ca(2+)_transporter P-type Ca(2+) transporter], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=7.2.2.10 7.2.2.10] </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=7bt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bt2 OCA], [http://pdbe.org/7bt2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7bt2 RCSB], [http://www.ebi.ac.uk/pdbsum/7bt2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7bt2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [[http://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 == | ||
| + | [[http://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 == | ||
| + | Under physiological conditions, most Ca(2+)-ATPase (SERCA) molecules bind ATP before binding the Ca(2+) transported. SERCA has a high affinity for ATP even in the absence of Ca(2+), and ATP accelerates Ca(2+) binding at pH values lower than 7, where SERCA is in the E2 state with low-affinity Ca(2+)-binding sites. Here we describe the crystal structure of SERCA2a, the isoform predominant in cardiac muscle, in the E2.ATP state at 3.0-A resolution. In the crystal structure, the arrangement of the cytoplasmic domains is distinctly different from that in canonical E2. The A-domain now takes an E1 position, and the N-domain occupies exactly the same position as that in the E1.ATP.2Ca(2+) state relative to the P-domain. As a result, ATP is properly delivered to the phosphorylation site. Yet phosphoryl transfer never takes place without the filling of the two transmembrane Ca(2+)-binding sites. The present crystal structure explains what ATP binding itself does to SERCA and how nonproductive phosphorylation is prevented in E2. | ||
| + | |||
| + | What ATP binding does to the Ca(2+) pump and how nonproductive phosphoryl transfer is prevented in the absence of Ca(2).,Kabashima Y, Ogawa H, Nakajima R, Toyoshima C Proc Natl Acad Sci U S A. 2020 Jul 16. pii: 2006027117. doi:, 10.1073/pnas.2006027117. PMID:32675243<ref>PMID:32675243</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7bt2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Kabashima Y]] | + | [[Category: Kabashima, Y]] |
| - | [[Category: Nakajima R]] | + | [[Category: Nakajima, R]] |
| - | [[Category: Ogawa H]] | + | [[Category: Ogawa, H]] |
| - | [[Category: Toyoshima C]] | + | [[Category: Toyoshima, C]] |
| + | [[Category: Ca2+-atpase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: P-type atpase]] | ||
Revision as of 06:43, 19 August 2020
Crystal structure of the SERCA2a in the E2.ATP state
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