6iz3: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='6iz3' size='340' side='right'caption='[[6iz3]], [[Resolution|resolution]] 3.79Å' scene=''> | <StructureSection load='6iz3' size='340' side='right'caption='[[6iz3]], [[Resolution|resolution]] 3.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6iz3]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6iz3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IZ3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.791Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6iz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iz3 OCA], [https://pdbe.org/6iz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iz3 RCSB], [https://www.ebi.ac.uk/pdbsum/6iz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iz3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/T38BB_XENLA T38BB_XENLA] Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores.[UniProtKB:Q9DAV9] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Xenopus laevis]] | ||
[[Category: | [[Category: Chen YH]] | ||
[[Category: | [[Category: Su M]] | ||
[[Category: | [[Category: Wang XH]] | ||
[[Category: | [[Category: Zeng Y]] | ||
Latest revision as of 12:55, 22 November 2023
Structural basis for activity of TRIC counter-ion channels in calcium releaseStructural basis for activity of TRIC counter-ion channels in calcium release
Structural highlights
FunctionT38BB_XENLA Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores.[UniProtKB:Q9DAV9] Publication Abstract from PubMedTrimeric intracellular cation (TRIC) channels are thought to provide counter-ion currents that facilitate the active release of Ca(2+) from intracellular stores. TRIC activity is controlled by voltage and Ca(2+) modulation, but underlying mechanisms have remained unknown. Here we describe high-resolution crystal structures of vertebrate TRIC-A and TRIC-B channels, both in Ca(2+)-bound and Ca(2+)-free states, and we analyze conductance properties in structure-inspired mutagenesis experiments. The TRIC channels are symmetric trimers, wherein we find a pore in each protomer that is gated by a highly conserved lysine residue. In the resting state, Ca(2+) binding at the luminal surface of TRIC-A, on its threefold axis, stabilizes lysine blockage of the pores. During active Ca(2+) release, luminal Ca(2+) depletion removes inhibition to permit the lysine-bearing and voltage-sensing helix to move in response to consequent membrane hyperpolarization. Diacylglycerol is found at interprotomer interfaces, suggesting a role in metabolic control. Structural basis for activity of TRIC counter-ion channels in calcium release.,Wang XH, Su M, Gao F, Xie W, Zeng Y, Li DL, Liu XL, Zhao H, Qin L, Li F, Liu Q, Clarke OB, Lam SM, Shui GH, Hendrickson WA, Chen YH Proc Natl Acad Sci U S A. 2019 Feb 15. pii: 1817271116. doi:, 10.1073/pnas.1817271116. PMID:30770441[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||