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Protein-phospholipid interplay revealed with crystals of a calcium pump
Nature (London), 2017-05, Vol.545 (7653), p.193-198
[Peer Reviewed Journal]
Copyright Nature Publishing Group May 11, 2017 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/nature22357 ;PMID: 28467821
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Title:
Protein-phospholipid interplay revealed with crystals of a calcium pump
Author:
Norimatsu, Yoshiyuki
;
Hasegawa, Kazuya
;
Shimizu, Nobutaka
;
Toyoshima, Chikashi
Subjects:
Adenosine diphosphate
;
Arginine - metabolism
;
ATP
;
Biochemistry
;
Ca2+-transporting ATPase
;
Calcium
;
Calcium (reticular)
;
Calcium - metabolism
;
Calcium ions
;
Calcium signalling
;
Calcium-Transporting ATPases - chemistry
;
Calcium-Transporting ATPases - metabolism
;
Cell culture
;
Crystallization
;
Crystallography
;
Crystallography, X-Ray
;
Crystals
;
Cytoplasm
;
Cytoplasm - metabolism
;
Data collection
;
Density
;
Dephosphorylation
;
Diffraction
;
Electron density
;
Energy costs
;
Helices
;
Ion pumps
;
Lecithin
;
Lipid bilayers
;
Lipid Bilayers - chemistry
;
Lipid Bilayers - metabolism
;
Lipids
;
Lysine - metabolism
;
Macromolecules
;
Membrane proteins
;
Membranes
;
Models, Molecular
;
Molecular biology
;
Molecular modelling
;
Na+/K+-exchanging ATPase
;
Phosphates
;
Phospholipids
;
Phospholipids - chemistry
;
Phospholipids - metabolism
;
Protein Conformation
;
Proteins
;
Pumps
;
Radiation
;
Radiation research
;
Residues
;
Science and technology
;
Translocation
;
Tryptophan - metabolism
;
Visual perception
Is Part Of:
Nature (London), 2017-05, Vol.545 (7653), p.193-198
Description:
The lipid bilayer has so far eluded visualization by conventional crystallographic methods, severely limiting our understanding of phospholipid- and protein-phospholipid interactions. Here we describe electron density maps for crystals of Ca -ATPase in four different states obtained by X-ray solvent contrast modulation. These maps resolve the entire first layer of phospholipids surrounding the transmembrane helices, although less than half of them are hydrogen-bonded to protein residues. Phospholipids follow the movements of associated residues, causing local distortions and changes in thickness of the bilayer. Unexpectedly, the entire protein tilts during the reaction cycle, governed primarily by a belt of Trp residues, to minimize energy costs accompanying the large perpendicular movements of the transmembrane helices. A class of Arg residues extend their side chains through the cytoplasm to exploit phospholipids as anchors for conformational switching. Thus, phospholipid-Arg/Lys and phospholipid-Trp interactions have distinct functional roles in the dynamics of ion pumps and, presumably, membrane proteins in general.
Publisher:
England: Nature Publishing Group
Language:
English
Identifier:
ISSN: 0028-0836
EISSN: 1476-4687
DOI: 10.1038/nature22357
PMID: 28467821
Source:
ProQuest One Psychology
MEDLINE
ProQuest Central
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