7k0t

<table><tr><td colspan='2'>[[7k0t]] is a 4 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=7K0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K0T FirstGlance]. <br>

</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=ZN:ZINC+ION'>ZN</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7tdg|7tdg]]</div></td></tr>

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== Publication Abstract from PubMed ==

Activation of the intracellular Ca(2+) channel ryanodine receptor (RyR) triggers a cytosolic Ca(2+) surge, while elevated cytosolic Ca(2+) inhibits the channel in a negative feedback mechanism. Cryo-EM of rabbit RyR1 embedded in nanodiscs under partially inactivating Ca(2+) conditions revealed an open and a closed-inactivated conformation. Ca(2+) binding to the high affinity site engages the central and C-terminal domains into a block, which pries the S6 four-helix bundle open. Further rotation of this block pushes S6 toward the central axis, closing (inactivating) the channel. Main characteristics of the Ca(2+)-inactivated conformation are downward conformation of the cytoplasmic assembly and tightly-knit subunit interface contributed by a fully occupied Ca(2+) activation site, two inter-subunit resolved lipids, and two salt bridges between the EF hand domain and the S2-S3 loop validated by disease-causing mutations. The structural insight illustrates the prior Ca(2+) activation prerequisite for Ca(2+) inactivation and provides for seamless transition from inactivated to closed conformations.

Ca(2+)-inactivation of the mammalian ryanodine receptor type 1 in a lipidic environment revealed by cryo-EM.,Nayak AR, Samso M Elife. 2022 Mar 8;11. pii: 75568. doi: 10.7554/eLife.75568. PMID:35257661<ref>PMID:35257661</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Nayak, A R]]

[[Category: Samso, M]]

[[Category: Transport protein]]