2kyv: Difference between revisions
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==Hybrid solution and solid-state NMR structure ensemble of phospholamban pentamer== | ==Hybrid solution and solid-state NMR structure ensemble of phospholamban pentamer== | ||
<StructureSection load='2kyv' size='340' side='right'caption='[[2kyv | <StructureSection load='2kyv' size='340' side='right'caption='[[2kyv]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2kyv]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2kyv]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KYV FirstGlance]. <br> | ||
</td></tr> | </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=2kyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kyv OCA], [https://pdbe.org/2kyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kyv RCSB], [https://www.ebi.ac.uk/pdbsum/2kyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kyv ProSAT]</span></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=2kyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kyv OCA], [https://pdbe.org/2kyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kyv RCSB], [https://www.ebi.ac.uk/pdbsum/2kyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kyv ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/PPLA_RABIT PPLA_RABIT] Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulum. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Shi | [[Category: Shi L]] | ||
[[Category: Traaseth | [[Category: Traaseth NJ]] | ||
[[Category: Veglia | [[Category: Veglia G]] | ||
[[Category: Verardi | [[Category: Verardi R]] | ||
Revision as of 11:09, 18 January 2023
Hybrid solution and solid-state NMR structure ensemble of phospholamban pentamerHybrid solution and solid-state NMR structure ensemble of phospholamban pentamer
Structural highlights
FunctionPPLA_RABIT Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulum. Publication Abstract from PubMedPhospholamban (PLN) is a type II membrane protein that inhibits the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA), thereby regulating calcium homeostasis in cardiac muscle. In membranes, PLN forms pentamers that have been proposed to function either as a storage for active monomers or as ion channels. Here, we report the T-state structure of pentameric PLN solved by a hybrid solution and solid-state NMR method. In lipid bilayers, PLN adopts a pinwheel topology with a narrow hydrophobic pore, which excludes ion transport. In the T state, the cytoplasmic amphipathic helices (domains Ia) are absorbed into the lipid bilayer with the transmembrane domains arranged in a left-handed coiled-coil configuration, crossing the bilayer with a tilt angle of approximately 11 degrees with respect to the membrane normal. The tilt angle difference between the monomer and pentamer is approximately 13 degrees , showing that intramembrane helix-helix association forces dominate over the hydrophobic mismatch, driving the overall topology of the transmembrane assembly. Our data reveal that both topology and function of PLN are shaped by the interactions with lipids, which fine-tune the regulation of SERCA. Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.,Verardi R, Shi L, Traaseth NJ, Walsh N, Veglia G Proc Natl Acad Sci U S A. 2011 May 31;108(22):9101-6. Epub 2011 May 16. PMID:21576492[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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