2YFY

SERCA in the HnE2 State Complexed With Debutanoyl Thapsigargin

2YFY の概要

• エントリーDOI: 10.2210/pdb2yfy/pdb
• 関連するPDBエントリー: 1FQU 1IWO 1KJU 1SU4 1T5S 1T5T 1VFP 1WPG 1XP5 2AGV 2BY4 2C88 2C8K 2C8L 2C9M 2VOY
• 分子名称: SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1, DEBUTANOYL THAPSIGARGIN, POTASSIUM ION, ... (4 entities in total)
• 機能のキーワード: membrane protein, serca, p-type atpase, prostate cancer, hydrolase, ion transport
• 由来する生物種: ORYCTOLAGUS CUNICULUS (RABBIT)
• 細胞内の位置: Endoplasmic reticulum membrane; Multi-pass membrane protein: P04191
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 110246.64

構造登録者

Sonntag, Y.,Musgaard, M.,Olesen, C.,Schiott, B.,Moller, J.V.,Nissen, P.,Thogersen, L. (登録日: 2011-04-11, 公開日: 2011-06-29, 最終更新日: 2025-10-01)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.1 Å)