8ghf: Difference between revisions
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==cryo-EM structure of hSlo1 in plasma membrane vesicles== | |||
<StructureSection load='8ghf' size='340' side='right'caption='[[8ghf]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ghf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GHF 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=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=POV:(2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>POV</scene></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=8ghf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ghf OCA], [https://pdbe.org/8ghf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ghf RCSB], [https://www.ebi.ac.uk/pdbsum/8ghf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ghf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KCMA1_HUMAN KCMA1_HUMAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Integral membrane protein structure determination traditionally requires extraction from cell membranes using detergents or polymers. Here, we describe the isolation and structure determination of proteins in membrane vesicles derived directly from cells. Structures of the ion channel Slo1 from total cell membranes and from cell plasma membranes were determined at 3.8 A and 2.7 A resolution, respectively. The plasma membrane environment stabilizes Slo1, revealing an alteration of global helical packing, polar lipid, and cholesterol interactions that stabilize previously unresolved regions of the channel and an additional ion binding site in the Ca(2+) regulatory domain. The two methods presented enable structural analysis of both internal and plasma membrane proteins without disrupting weakly interacting proteins, lipids, and cofactors that are essential to biological function. | |||
Membrane protein isolation and structure determination in cell-derived membrane vesicles.,Tao X, Zhao C, MacKinnon R Proc Natl Acad Sci U S A. 2023 May 2;120(18):e2302325120. doi: , 10.1073/pnas.2302325120. Epub 2023 Apr 25. PMID:37098056<ref>PMID:37098056</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8ghf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: MacKinnon R]] | |||
[[Category: Tao X]] | |||
[[Category: Zhao C]] | |||
Revision as of 09:57, 10 May 2023
cryo-EM structure of hSlo1 in plasma membrane vesiclescryo-EM structure of hSlo1 in plasma membrane vesicles
Structural highlights
FunctionPublication Abstract from PubMedIntegral membrane protein structure determination traditionally requires extraction from cell membranes using detergents or polymers. Here, we describe the isolation and structure determination of proteins in membrane vesicles derived directly from cells. Structures of the ion channel Slo1 from total cell membranes and from cell plasma membranes were determined at 3.8 A and 2.7 A resolution, respectively. The plasma membrane environment stabilizes Slo1, revealing an alteration of global helical packing, polar lipid, and cholesterol interactions that stabilize previously unresolved regions of the channel and an additional ion binding site in the Ca(2+) regulatory domain. The two methods presented enable structural analysis of both internal and plasma membrane proteins without disrupting weakly interacting proteins, lipids, and cofactors that are essential to biological function. Membrane protein isolation and structure determination in cell-derived membrane vesicles.,Tao X, Zhao C, MacKinnon R Proc Natl Acad Sci U S A. 2023 May 2;120(18):e2302325120. doi: , 10.1073/pnas.2302325120. Epub 2023 Apr 25. PMID:37098056[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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