2KYV

Hybrid solution and solid-state NMR structure ensemble of phospholamban pentamer

Summary for 2KYV

• Entry DOI: 10.2210/pdb2kyv/pdb
• Related: 2KB7 2M3B
• Descriptor: Phospholamban (1 entity in total)
• Functional Keywords: phospholamban, membrane protein, solid state nmr, hybrid method
• Biological source: Escherichia coli
• Total number of polymer chains: 5
• Total formula weight: 30497.49

Authors

Verardi, R.,Shi, L.,Traaseth, N.J.,Veglia, G. (deposition date: 2010-06-08, release date: 2011-05-11, Last modification date: 2024-05-01)

Primary citation

Verardi, R.,Shi, L.,Traaseth, N.J.,Walsh, N.,Veglia, G.
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.
Proc.Natl.Acad.Sci.USA, 108:9101-9106, 2011

PubMed Abstract: Phospholamban (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° with respect to the membrane normal. The tilt angle difference between the monomer and pentamer is approximately 13°, 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.

PubMed: 21576492
DOI: 10.1073/pnas.1016535108

Experimental method

SOLID-STATE NMR
SOLUTION NMR