2YFY

SERCA in the HnE2 State Complexed With Debutanoyl Thapsigargin

Summary for 2YFY

• Entry DOI: 10.2210/pdb2yfy/pdb
• Related: 1FQU 1IWO 1KJU 1SU4 1T5S 1T5T 1VFP 1WPG 1XP5 2AGV 2BY4 2C88 2C8K 2C8L 2C9M 2VOY
• Descriptor: SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1, DEBUTANOYL THAPSIGARGIN, POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: membrane protein, serca, p-type atpase, prostate cancer, hydrolase, ion transport
• Biological source: ORYCTOLAGUS CUNICULUS (RABBIT)
• Cellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein: P04191
• Total number of polymer chains: 1
• Total formula weight: 110246.64

Authors

Sonntag, Y.,Musgaard, M.,Olesen, C.,Schiott, B.,Moller, J.V.,Nissen, P.,Thogersen, L. (deposition date: 2011-04-11, release date: 2011-06-29, Last modification date: 2025-10-01)

Primary citation

Sonntag, Y.,Musgaard, M.,Olesen, C.,Schiott, B.,Moller, J.V.,Nissen, P.,Thogersen, L.
Mutual Adaptation of a Membrane Protein and its Lipid Bilayer During Conformational Changes.
Nat.Commun., 2:304-, 2011

PubMed Abstract: The structural elucidation of membrane proteins continues to gather pace, but we know little about their molecular interactions with the lipid environment or how they interact with the surrounding bilayer. Here, with the aid of low-resolution X-ray crystallography, we present direct structural information on membrane interfaces as delineated by lipid phosphate groups surrounding the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) in its phosphorylated and dephosphorylated Ca(2+)-free forms. The protein-lipid interactions are further analysed using molecular dynamics simulations. We find that SERCA adapts to membranes of different hydrophobic thicknesses by inducing local deformations in the lipid bilayers and by undergoing small rearrangements of the amino-acid side chains and helix tilts. These mutually adaptive interactions allow smooth transitions through large conformational changes associated with the transport cycle of SERCA, a strategy that may be of general nature for many membrane proteins.

PubMed: 21556058
DOI: 10.1038/NCOMMS1307

Experimental method

X-RAY DIFFRACTION (3.1 Å)