Review
Lipids in membrane protein structures

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Abstract

This review describes the recent knowledge about tightly bound lipids in membrane protein structures and deduces general principles of the binding interactions. Bound lipids are grouped in annular, nonannular, and integral protein lipids. The importance of lipid binding for vertical positioning and tight integration of proteins in the membrane, for assembly and stabilization of oligomeric and multisubunit complexes, for supercomplexes, as well as their functional roles are pointed out. Lipid binding is stabilized by multiple noncovalent interactions from protein residues to lipid head groups and hydrophobic tails. Based on analysis of lipids with refined head groups in membrane protein structures, distinct motifs were identified for stabilizing interactions between the phosphodiester moieties and side chains of amino acid residues. Differences between binding at the electropositive and electronegative membrane side, as well as a preferential binding to the latter, are observed. A first attempt to identify lipid head group specific binding motifs is made. A newly identified cardiolipin binding site in the yeast cytochrome bc1 complex is described. Assignment of unsaturated lipid chains and evolutionary aspects of lipid binding are discussed.

Abbreviations

BC1
cytochrome bc1 complex
B6F
cytochrome b6f complex
COX
cytochrome c oxidase
RC
photosynthetic reaction center
PSI
Photosystem I
BR
bacteriorhodopsin
AC
ADP/ATP carrier
FDH
formate dehydrogenase N
SDH
succinate dehydrogenase
PE
phosphatidyl ethanolamine
PC
phosphatidyl choline
PI
phosphatidyl inositol
PG
phosphatidyl glycerol
CL
cardiolipin
DG
phosphatidylglycerophospholipid
SL
sulfolipid
PA
phosphatidic acid
PS
phosphatidylserine
EPR
electron paramagnetic resonance
IMM
inner mitochondrial membrane
IMS
intermembrane space
UM
undecyl maltopyranose

Keywords

Lipid
Membrane protein
Lipid–protein interaction
X-ray structure
Phospholipid
Cardiolipin

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