X-Ray Crystallographic Analysis of Lipid-Protein Interactions in the Bacteriorhodopsin Purple Membrane

2003 ◽  
Vol 32 (1) ◽  
pp. 285-310 ◽  
Author(s):  
Jean-Philippe Cartailler ◽  
Hartmut Luecke
Keyword(s):  
Protein Interactions ◽  
Crystallographic Analysis ◽  
Purple Membrane ◽  
X Ray ◽  
Lipid Protein Interactions

Specific lipid–protein interactions in a novel honeycomb lattice structure of bacteriorhodopsin

1999 ◽  
Vol 55 (7) ◽  
pp. 1251-1256 ◽  
Author(s):  
Hidenori Sato ◽  
Kazuki Takeda ◽  
Koji Tani ◽  
Tomoya Hino ◽  
Tetsuji Okada ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Lattice Structure ◽  
Hexagonal Lattice ◽  
Crystallographic Analysis ◽  
Purple Membrane ◽  
Honeycomb Lattice ◽  
Vesicular Structure ◽  
Lipid Protein Interactions ◽  
Planar Membranes ◽  
Inside Out

In the purple membrane of Halobacterium salinarium, bacteriorhodopsin trimers are arranged in a hexagonal lattice. When purple membrane sheets are incubated at high temperature with neutral detergent, membrane vesicularization takes place, yielding inside-out vesicles with a diameter of 50 nm. The vesicular structure becomes unstable at low temperature, where successive fusion of the vesicles yields a crystal which is composed of stacked planar membranes. X-ray crystallographic analysis reveals that the bacteriorhodopsin trimers are arranged in a honeycomb lattice in each membrane layer and that neighbouring membranes orient in opposite directions. The native structure of the trimeric unit is preserved in the honeycomb lattice, irrespective of alterations in the in-plane orientation of the trimer. One phospholipid tightly bound to a crevice between monomers in the trimeric unit is suggested to act as a glue in the formation of the trimer.

LIPID-PROTEIN INTERACTIONS IN THE PURPLE MEMBRANE

1978 ◽  
pp. 141-155 ◽  
Author(s):  
Patricia C. Jost ◽  
Debra A. McMillen ◽  
William D. Morgan ◽  
Walther Stoeckenius
Keyword(s):  
Protein Interactions ◽  
Purple Membrane ◽  
Lipid Protein Interactions

The Incorporation of Lung Surfactant Specific Protein SP-B Into Lipid Monolayers at the Air-Fluid Interface: A Grazing Incidence x-ray Diffraction Study

1999 ◽  
Vol 590 ◽  
Author(s):  
K.Y.C. Lee ◽  
J. Majewski ◽  
T.L. Kuhl ◽  
P.B. Howes ◽  
K. Kjaer ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Lung Surfactant ◽  
Grazing Incidence ◽  
Specific Protein ◽  
Fluid Interface ◽  
X Ray Diffraction ◽  
X Ray ◽  
Disordered Phase ◽  
Lipid Protein Interactions ◽  
Plane Diffraction

ABSTRACTGrazing incidence x-ray diffraction (GIXD) measurements were performed to determine the effects of SP-B1.25, the N-terminus peptide of lung surfactant specific protein SP-B1.25, on the structure of palmitic acid (PA) monolayers. In-plane diffraction shows that the peptide fluidizes a portion of the monolayer, but does not affect the packing of the residual ordered phase. This implies that the peptide resides in the disordered phase, and that the ordered phase is essentially pure lipid. The quantitative insights afforded by this study lead to a better understanding of the lipid/protein interactions found in lung surfactant systems.

A refinement analysis of the crystallography of the phospholipid, 1,2-dilauroyl-DL-phosphatidylethanolamine, and some remarks on lipid—lipid and lipid-protein interactions

1977 ◽  
Vol 354 (1677) ◽  
pp. 157-170 ◽  
Keyword(s):  
Electron Microscopy ◽  
Acetic Acid ◽  
Single Crystal ◽  
Least Squares ◽  
Protein Interactions ◽  
Halobacterium Halobium ◽  
X Ray Diffraction ◽  
X Ray ◽  
Bond Lengths ◽  
Lipid Protein Interactions

A least-squares refinement analysis of atomic positional and thermal parameters in a single crystal of 1,2-dilauroyl-DL-phosphatidylethanolamine: acetic acid has been based on the X-ray diffraction intensities of 1132 independent reflexions, assessed by automatic microdensitometry. The final unweighted discrepancy index is 0.16 with e.s.ds of the bond lengths ranging from 0.02 to 0.12 A. The general features of our earlier, lessprecise analysis are confirmed. The close-packed arrangement of the phospholipid molecules is discussed in relation to electron microscopy and diffraction studies of the structures of membranes from Acholeplasma laidlawii and Halobacterium halobium.

scholarly journals Computational Molecular Docking and X-ray Crystallographic Studies of Catechins in New Drug Design Strategies

Molecules ◽  
2018 ◽  
Vol 23 (8) ◽  
pp. 2020 ◽  
Author(s):  
Shogo Nakano ◽  
Shin-ichi Megro ◽  
Tadashi Hase ◽  
Takuji Suzuki ◽  
Mamoru Isemura ◽  
...  
Keyword(s):  
Green Tea ◽  
Protein Interactions ◽  
Crystallographic Analysis ◽  
New Drugs ◽  
Hydroxyl Groups ◽  
Epicatechin Gallate ◽  
Tea Catechins ◽  
Computational Docking ◽  
X Ray ◽  
Green Tea Catechins

Epidemiological and laboratory studies have shown that green tea and green tea catechins exert beneficial effects on a variety of diseases, including cancer, metabolic syndrome, infectious diseases, and neurodegenerative diseases. In most cases, (−)-epigallocatechin gallate (EGCG) has been shown to play a central role in these effects by green tea. Catechins from other plant sources have also shown health benefits. Many studies have revealed that the binding of EGCG and other catechins to proteins is involved in its action mechanism. Computational docking analysis (CMDA) and X-ray crystallographic analysis (XCA) have provided detailed information on catechin-protein interactions. Several of these studies have revealed that the galloyl moiety anchors it to the cleft of proteins through interactions with its hydroxyl groups, explaining the higher activity of galloylated catechins such as EGCG and epicatechin gallate than non-galloylated catechins. In this paper, we review the results of CMDA and XCA of EGCG and other plant catechins to understand catechin-protein interactions with the expectation of developing new drugs with health-promoting properties.

Quaternary structure of Limulus polyphemus hemocyanin

1978 ◽  
Vol 36 (2) ◽  
pp. 176-177
Author(s):  
T. Wichertjes ◽  
E.J. Kwak ◽  
E.F.J. Van Bruggen
Keyword(s):  
Electron Microscopy ◽  
Functional Properties ◽  
Horseshoe Crab ◽  
Temperature Jump ◽  
Quaternary Structure ◽  
Crystallographic Analysis ◽  
Limulus Polyphemus ◽  
Oxygen Binding ◽  
X Ray ◽  
Intact Molecule

Hemocyanin of the horseshoe crab (Limulus polyphemus) has been studied in nany ways. Recently the structure, dissociation and reassembly was studied using electron microscopy of negatively stained specimens as the method of investigation. Crystallization of the protein proved to be possible and X-ray crystallographic analysis was started. Also fluorescence properties of the hemocyanin after dialysis against Tris-glycine buffer + 0.01 M EDTA pH 8.9 (so called “stripped” hemocyanin) and its fractions II and V were studied, as well as functional properties of the fractions by NMR. Finally the temperature-jump method was used for assaying the oxygen binding of the dissociating molecule and of preparations of isolated subunits. Nevertheless very little is known about the structure of the intact molecule. Schutter et al. suggested that the molecule possibly consists of two halves, combined in a staggered way, the halves themselves consisting of four subunits arranged in a square.

Difference Fourier Analysis of Glucose Embedded and Frozen Hydrated Purple Membrane

1982 ◽  
Vol 40 ◽  
pp. 74-75
Author(s):  
Jules S. Jaffe ◽  
Robert M. Glaeser
Keyword(s):  
Purple Membrane ◽  
Data Set ◽  
High Resolution Data ◽  
X Ray ◽  
X Ray Crystallography ◽  
Fourier Techniques ◽  
Versus Protein ◽  
The Difference ◽  
Difference Fourier ◽  
Ideal Method

Although difference Fourier techniques are standard in X-ray crystallography it has only been very recently that electron crystallographers have been able to take advantage of this method. We have combined a high resolution data set for frozen glucose embedded Purple Membrane (PM) with a data set collected from PM prepared in the frozen hydrated state in order to visualize any differences in structure due to the different methods of preparation. The increased contrast between protein-ice versus protein-glucose may prove to be an advantage of the frozen hydrated technique for visualizing those parts of bacteriorhodopsin that are embedded in glucose. In addition, surface groups of the protein may be disordered in glucose and ordered in the frozen state. The sensitivity of the difference Fourier technique to small changes in structure provides an ideal method for testing this hypothesis.

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