7bt2: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==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]] 3.00&Aring;' scene=''>
 == 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>
+== 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&reg;/PubMed&reg;, 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__
 </StructureSection>
+[[Category: Human]]
 [[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]]