Lipids in membrane protein structures

Pálsdóttir, Hildur; Hunte, Carola

doi:10.1016/j.bbamem.2004.06.012

Cited by 394 publications

(366 citation statements)

References 102 publications

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“…7–9). Lipids are known to play important roles in membrane enzyme complexes 34,35 and can mediate transient multimerization of membrane proteins 36 . A recent cryo-EM structure showed that lipids are involved in the assembly of the heterotetrameric γ-secretase 37 .…”

Section: Introductionmentioning

confidence: 99%

The atomic structure of a eukaryotic oligosaccharyltransferase complex

Bai

Wang

Zhao

et al. 2018

Nature

103

131

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SUMMARY N-glycosylation is a ubiquitous modification of eukaryotic secretory and membrane-bound proteins; about 90% of glycoproteins are N-glycosylated. The reaction is catalyzed by an eight-protein oligosaccharyltransferase complex, OST, embedded in the ER membrane. Our understanding of eukaryotic protein N-glycosylation has been limited due to the lack of high-resolution structures. Here we report a 3.5-Å resolution cryo-EM structure of the Saccharomyces cerevisiae OST, revealing the structures of Ost1–5, Stt3, Wbp1, and Swp1. We found that seven phospholipids mediate many of the inter-subunit interactions, and an Stt3 N-glycan mediates interaction with Wbp1 and Swp1 in the lumen. Ost3 was found to mediate the OST-Sec61 translocon interface, funneling the acceptor peptide towards the OST catalytic site as the nascent peptide emerges from the translocon. The structure provides novel insights into co-translational protein N-glycosylation and may facilitate the development of small-molecule inhibitors targeting this process.

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Section: Introductionmentioning

confidence: 99%

The atomic structure of a eukaryotic oligosaccharyltransferase complex

Bai

Wang

Zhao

et al. 2018

Nature

103

131

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“…Since a significant portion of integral membrane proteins remains in contact with the membrane lipids, 1 the structure and function of membrane proteins often depend on their interactions with the surrounding lipids. 2 The lipid composition of cells that make up the nervous system is unique and has been correlated with increased complexity in the organization of the nervous system during evolution. 3 The organization and dynamics of cellular membranes in the nervous system play a crucial role in the function of neuronal membrane receptors.…”

Section: Introductionmentioning

confidence: 99%

Exploring the Organization and Dynamics of Hippocampal Membranes Utilizing Pyrene Fluorescence

2008

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The organization and dynamics of cellular membranes in the nervous system are crucial for the function of neuronal membrane receptors and signal transduction. Previous work from our laboratory has established hippocampal membranes as a convenient natural source for studying neuronal receptors. In this paper, we have monitored the organization and dynamics of hippocampal membranes and their modulation by cholesterol using pyrene fluorescence. The apparent dielectric constant experienced by pyrene in hippocampal membranes turns out to be ∼20 ( 3, depending on the experimental condition. Our results show that the polarity of the hippocampal membrane is increased upon cholesterol depletion, as monitored by changes in the ratio of pyrene vibronic peak intensities (I 1 /I 3 ). This is accompanied by an increase in lateral diffusion, measured as an increase in the pyrene excimer/monomer ratio. These results are relevant in understanding the complex organization and dynamics of hippocampal membranes and could have implications in neuronal diseases characterized by defective cholesterol metabolism.

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“…A recent study analyzed the binding specificity of the phosphodiester group using 30 unique, ordered lipids seen in x-ray structures [5]. These lipids had been co-purified with the protein, indicating that they are strongly and specifically bound.…”

Section: Lipid-protein Interactionsmentioning

confidence: 99%

“…These lipids have typically originated from the native membrane and have co-purified with the protein. Analysis of such tightly bound lipids has provided insight into the specific binding of lipids to membrane proteins [5].…”

Section: Introductionmentioning

confidence: 99%

Interactions of lipids with aquaporin-0 and other membrane proteins

Hite

Gonen

Walz

2007

Pflugers Arch - Eur J Physiol

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The structure of aquaporin-0 (AQP0) has recently been determined by electron crystallography of two-dimensional (2D) crystals and by x-ray crystallography of three-dimensional (3D) crystals. The electron crystallographic structure revealed nine lipids per AQP0 monomer, which form an almost complete bilayer. The lipids adopt a wide variety of conformations and tightly fill the space between adjacent AQP0 tetramers. The conformations of the lipid acyl chains appear to be determined not only by the protein surface but also by the acyl chains of adjacent lipid molecules. In the x-ray structure, the hydrophobic region of the protein is surrounded by a detergent micelle, with two ordered detergent molecules per AQP0 monomer. Despite the different environments, the electron crystallographic and x-ray structures of AQP0 are virtually identical, but they differ in the temperature factors of the atoms that either contact the lipids in the 2D crystals or are exposed to detergents in the 3D crystals. The temperature factors are higher in the x-ray structure, suggesting that the detergent-exposed AQP0 residues are less ordered than the corresponding ones contacting lipids in the 2D crystals. An examination of ordered detergent molecules in crystal structures of other aquaporins and of lipid molecules in 2D and 3D crystals of bacteriorhodopsin suggests that the increased conformational variability of detergent-exposed residues compared to lipid-contacting residues is a general feature.

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Lipids in membrane protein structures

Cited by 394 publications

References 102 publications

The atomic structure of a eukaryotic oligosaccharyltransferase complex

The atomic structure of a eukaryotic oligosaccharyltransferase complex

Exploring the Organization and Dynamics of Hippocampal Membranes Utilizing Pyrene Fluorescence

Interactions of lipids with aquaporin-0 and other membrane proteins

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