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| <SX load='5taz' size='340' side='right' viewer='molstar' caption='[[5taz]], [[Resolution|resolution]] 4.30Å' scene=''> | | <SX load='5taz' size='340' side='right' viewer='molstar' caption='[[5taz]], [[Resolution|resolution]] 4.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5taz]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TAZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TAZ FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5taz]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TAZ 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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 4.3Å</td></tr> |
| <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5t15|5t15]], [[5t9m|5t9m]], [[5t9n|5t9n]], [[5t9r|5t9r]], [[5t9s|5t9s]], [[5t9v|5t9v]], [[5ta3|5ta3]], [[5tal|5tal]], [[5tam|5tam]], [[5tan|5tan]], [[5taq|5taq]], [[5tap|5tap]], [[5tas|5tas]], [[5tat|5tat]], [[5tau|5tau]], [[5tav|5tav]], [[5taw|5taw]], [[5tax|5tax]], [[5tay|5tay]], [[5tb0|5tb0]], [[5tb1|5tb1]], [[5tb2|5tb2]], [[5tb3|5tb3]], [[5tb4|5tb4]]</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=5taz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5taz OCA], [https://pdbe.org/5taz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5taz RCSB], [https://www.ebi.ac.uk/pdbsum/5taz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5taz ProSAT]</span></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP1B, FKBP12.6, FKBP1L, FKBP9, OTK4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5taz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5taz OCA], [http://pdbe.org/5taz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5taz RCSB], [http://www.ebi.ac.uk/pdbsum/5taz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5taz ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/RYR1_RABIT RYR1_RABIT]] Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity).<ref>PMID:10388749</ref> <ref>PMID:22036948</ref> [[http://www.uniprot.org/uniprot/FKB1B_HUMAN FKB1B_HUMAN]] Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | | [https://www.uniprot.org/uniprot/FKB1B_HUMAN FKB1B_HUMAN] Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The type-1 ryanodine receptor (RyR1) is an intracellular calcium (Ca(2+)) release channel required for skeletal muscle contraction. Here, we present cryo-EM reconstructions of RyR1 in multiple functional states revealing the structural basis of channel gating and ligand-dependent activation. Binding sites for the channel activators Ca(2+), ATP, and caffeine were identified at interdomain interfaces of the C-terminal domain. Either ATP or Ca(2+) alone induces conformational changes in the cytoplasmic assembly ("priming"), without pore dilation. In contrast, in the presence of all three activating ligands, high-resolution reconstructions of open and closed states of RyR1 were obtained from the same sample, enabling analyses of conformational changes associated with gating. Gating involves global conformational changes in the cytosolic assembly accompanied by local changes in the transmembrane domain, which include bending of the S6 transmembrane segment and consequent pore dilation, displacement, and deformation of the S4-S5 linker and conformational changes in the pseudo-voltage-sensor domain.
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| Structural Basis for Gating and Activation of RyR1.,des Georges A, Clarke OB, Zalk R, Yuan Q, Condon KJ, Grassucci RA, Hendrickson WA, Marks AR, Frank J Cell. 2016 Sep 22;167(1):145-157.e17. doi: 10.1016/j.cell.2016.08.075. PMID:27662087<ref>PMID:27662087</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 5taz" style="background-color:#fffaf0;"></div>
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| ==See Also==
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| *[[Ryanodine receptor 3D structures|Ryanodine receptor 3D structures]]
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| [[Category: Peptidylprolyl isomerase]]
| | [[Category: Clarke OB]] |
| [[Category: Clarke, O B]] | | [[Category: Frank J]] |
| [[Category: Frank, J]] | | [[Category: Hendrickson WA]] |
| [[Category: Georges, A des]]
| | [[Category: Marks AR]] |
| [[Category: Hendrickson, W A]] | | [[Category: Zalk R]] |
| [[Category: Marks, A R]] | | [[Category: Des Georges A]] |
| [[Category: Zalk, R]] | |
| [[Category: Ca2+]] | |
| [[Category: Ec coupling]]
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| [[Category: Gating]]
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| [[Category: Ryr]]
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| [[Category: Transport protein-isomerase complex]]
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