7rxg: Difference between revisions
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==afTMEM16 in C18 lipid nanodiscs with MSP1E3 scaffold protein in the presence of Ca2+, full dimer== | ==afTMEM16 in C18 lipid nanodiscs with MSP1E3 scaffold protein in the presence of Ca2+, full dimer== | ||
<StructureSection load='7rxg' size='340' side='right'caption='[[7rxg]]' scene=''> | <StructureSection load='7rxg' size='340' side='right'caption='[[7rxg]], [[Resolution|resolution]] 2.28Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RXG FirstGlance]. <br> | <table><tr><td colspan='2'>[[7rxg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RXG FirstGlance]. <br> | ||
</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=7rxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rxg OCA], [https://pdbe.org/7rxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rxg RCSB], [https://www.ebi.ac.uk/pdbsum/7rxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rxg 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PGW:(1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>PGW</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;'>[[7rwj|7rwj]], [[7rx2|7rx2]], [[7rx3|7rx3]], [[7rxa|7rxa]], [[7rxb|7rxb]], [[7rxh|7rxh]]</div></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=7rxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rxg OCA], [https://pdbe.org/7rxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rxg RCSB], [https://www.ebi.ac.uk/pdbsum/7rxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rxg ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
TMEM16 scramblases dissipate the plasma membrane lipid asymmetry to activate multiple eukaryotic cellular pathways. Scrambling was proposed to occur with lipid headgroups moving between leaflets through a membrane-spanning hydrophilic groove. Direct information on lipid-groove interactions is lacking. We report the 2.3 A resolution cryogenic electron microscopy structure of the nanodisc-reconstituted Ca(2+)-bound afTMEM16 scramblase showing how rearrangement of individual lipids at the open pathway results in pronounced membrane thinning. Only the groove's intracellular vestibule contacts lipids, and mutagenesis suggests scrambling does not require specific protein-lipid interactions with the extracellular vestibule. We find scrambling can occur outside a closed groove in thinner membranes and is inhibited in thicker membranes, despite an open pathway. Our results show afTMEM16 thins the membrane to enable scrambling and that an open hydrophilic pathway is not a structural requirement to allow rapid transbilayer movement of lipids. This mechanism could be extended to other scramblases lacking a hydrophilic groove. | |||
TMEM16 scramblases thin the membrane to enable lipid scrambling.,Falzone ME, Feng Z, Alvarenga OE, Pan Y, Lee B, Cheng X, Fortea E, Scheuring S, Accardi A Nat Commun. 2022 May 11;13(1):2604. doi: 10.1038/s41467-022-30300-z. PMID:35562175<ref>PMID:35562175</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7rxg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Accardi A]] | [[Category: Accardi, A]] | ||
[[Category: Falzone | [[Category: Falzone, M E]] | ||
[[Category: Lipid scrambling]] | |||
[[Category: Lipid transport]] | |||
[[Category: Tmem16]] | |||
Revision as of 11:15, 25 May 2022
afTMEM16 in C18 lipid nanodiscs with MSP1E3 scaffold protein in the presence of Ca2+, full dimerafTMEM16 in C18 lipid nanodiscs with MSP1E3 scaffold protein in the presence of Ca2+, full dimer
Structural highlights
Publication Abstract from PubMedTMEM16 scramblases dissipate the plasma membrane lipid asymmetry to activate multiple eukaryotic cellular pathways. Scrambling was proposed to occur with lipid headgroups moving between leaflets through a membrane-spanning hydrophilic groove. Direct information on lipid-groove interactions is lacking. We report the 2.3 A resolution cryogenic electron microscopy structure of the nanodisc-reconstituted Ca(2+)-bound afTMEM16 scramblase showing how rearrangement of individual lipids at the open pathway results in pronounced membrane thinning. Only the groove's intracellular vestibule contacts lipids, and mutagenesis suggests scrambling does not require specific protein-lipid interactions with the extracellular vestibule. We find scrambling can occur outside a closed groove in thinner membranes and is inhibited in thicker membranes, despite an open pathway. Our results show afTMEM16 thins the membrane to enable scrambling and that an open hydrophilic pathway is not a structural requirement to allow rapid transbilayer movement of lipids. This mechanism could be extended to other scramblases lacking a hydrophilic groove. TMEM16 scramblases thin the membrane to enable lipid scrambling.,Falzone ME, Feng Z, Alvarenga OE, Pan Y, Lee B, Cheng X, Fortea E, Scheuring S, Accardi A Nat Commun. 2022 May 11;13(1):2604. doi: 10.1038/s41467-022-30300-z. PMID:35562175[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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