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| | <StructureSection load='4ycn' size='340' side='right'caption='[[4ycn]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='4ycn' size='340' side='right'caption='[[4ycn]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ycn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YCN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YCN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ycn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YCN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7BL:(4S,5E,8S,9E,11S,13E,15E,18R)-4-HYDROXY-8-METHOXY-9,11-DIMETHYL-18-[(1Z,4E)-2-METHYLHEXA-1,4-DIEN-1-YL]OXACYCLOOCTADECA-5,9,13,15-TETRAEN-2-ONE'>7BL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AME:N-ACETYLMETHIONINE'>AME</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7BL:(4S,5E,8S,9E,11S,13E,15E,18R)-4-HYDROXY-8-METHOXY-9,11-DIMETHYL-18-[(1Z,4E)-2-METHYLHEXA-1,4-DIEN-1-YL]OXACYCLOOCTADECA-5,9,13,15-TETRAEN-2-ONE'>7BL</scene>, <scene name='pdbligand=AME:N-ACETYLMETHIONINE'>AME</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ycm|4ycm]]</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=4ycn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ycn OCA], [https://pdbe.org/4ycn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ycn RCSB], [https://www.ebi.ac.uk/pdbsum/4ycn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ycn ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ycn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ycn OCA], [http://pdbe.org/4ycn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ycn RCSB], [http://www.ebi.ac.uk/pdbsum/4ycn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ycn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AT2A1_RABIT AT2A1_RABIT]] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity). | + | [https://www.uniprot.org/uniprot/AT2A1_RABIT AT2A1_RABIT] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Calcium-transporting ATPase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Morita, M]] | + | [[Category: Morita M]] |
| - | [[Category: Ogawa, H]] | + | [[Category: Ogawa H]] |
| - | [[Category: Ohno, O]] | + | [[Category: Ohno O]] |
| - | [[Category: Suenaga, K]] | + | [[Category: Suenaga K]] |
| - | [[Category: Toyoshima, C]] | + | [[Category: Toyoshima C]] |
| - | [[Category: Yamori, T]] | + | [[Category: Yamori T]] |
| - | [[Category: Ca2+]]
| + | |
| - | [[Category: Had fold]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ion pump]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: P-type atpase]]
| + | |
| Structural highlights
4ycn is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 3.5Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
AT2A1_RABIT This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity).
Publication Abstract from PubMed
Biselyngbyasides (BLSs), macrolides from a marine cyanobacterium, are cytotoxic natural products whose target molecule is unknown. Here we report that BLSs are high affinity (Ki approximately 10 nM) inhibitors of Ca(2+)-pumps with a unique binding mode. The crystal structures of the Ca(2+)-pump in complex with BLSs at 3.2-3.5 A-resolution show that BLSs bind to the pump near the cytoplasmic surface of the transmembrane region. The crystal structures and activity measurement of BLS analogs allow us to identify the structural features that confer high potency to BLSs as inhibitors of the pump.
Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca(2+) pumps with a unique mode of binding.,Morita M, Ogawa H, Ohno O, Yamori T, Suenaga K, Toyoshima C FEBS Lett. 2015 Jun 4;589(13):1406-11. doi: 10.1016/j.febslet.2015.04.056. Epub, 2015 May 6. PMID:25957767[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Morita M, Ogawa H, Ohno O, Yamori T, Suenaga K, Toyoshima C. Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca(2+) pumps with a unique mode of binding. FEBS Lett. 2015 Jun 4;589(13):1406-11. doi: 10.1016/j.febslet.2015.04.056. Epub, 2015 May 6. PMID:25957767 doi:http://dx.doi.org/10.1016/j.febslet.2015.04.056
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