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Bioinformatics for protein sequence, structure and function


Membrane Reference

Membrane Reference

References

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Legends

Figure 1

Bacteriorhodopsin. (A) 3D structure (PDB file 2BRD). The cytoplasmic side is down. The retinal is shown as a space-filling model, and lipids visible in the electron density are shown as ball and stick models. The cytoplasmic side is down. (B) Same as in A, but with charged residues shown as space-filling models. All 3D structure illustrations have been made using MOLSCRIPT (Kraulis, 1991).

Figure 2

Rhodopseudomonas viridis photosynthetic reaction center. (A) 3D structure (PDB file 1PRC). The cytoplasmic side is down. The extension of the lipid bilayer corresponds roughly to the large helix bundle in the lower part of the structure. Co-factors are shown as space-filling models. (B) Same as in A, but with Trp and Tyr residues shown as space-filling models.

Figure 3

Plant light-harvesting chlorophyll a/b-protein(courtesy of Dr. W. KŸhlbrandt, Heidelberg). The stromal side is down. The long N- and C-terminal helices are tilted by about 300 in the membrane whereas the shorter middle helix is less tilted. Chlorophylls and carotenoid molecules are shown as ball-and-stick models. Since the loops connecting the helices are not well-defined, they have been omitted from the structure.

Figure 4

One a and one § subunit from the Rhodopseudomonas acidophila light-harvesting antenna complex (courtesy of Dr. R.J. Cogdell, Glasgow). In the full complex, 9 a subunits form and inner ring separated from an outer ring of 9 § subunits by bacteriochlorophylls and carotenoid molecules (shown as ball-and-stick models). The cytoplasmic side is down.

Figure 5

Bovine mitochondrial cytochrome c oxidase (courtesy of Dr. Tomitake Tsukihara, Osaka and Dr. Shinya Yoshikawa, Hyogo). The matrix side is down.

Figure 6

Rhodobacter capsulata outer membrane porin. (A) 3D structure (PDB file 2POR) viewed in the plane of the membrane. The periplasmic side is down. Aromatic residues (Phe, Trp, Tyr) are shown as space-filling models. (B) View from outside the membrane. Note the internal loop that controls the pore properties.

Figure 7

Ovine prostaglandin H2 synthase-1 (PDB file 1PRH). Note the cluster of exposed hydrophobic residues on the bottom a-helices (shown as space-filling models) believed to anchor the molecule in the lumenal leaflet of the ER membrane.

Figure 8

The soluble form of colicin A (PDB file 1COL). The molecule is viewed from the side believed to bind to the bacterial membrane, i.e., the view is as seen by the victim. The hydrophobic helical hairpin (viewed on end) is sandwiched between two layers of helices that protect it from contact with water. Upon membrane binding, the helical hairpin is though to insert into the lipid bilayer.

Figure 9

Glycophorin A. (A) Helical net plot of the transmembrane helix. The packing interface is encircled. (B) 3D model for the transmembrane helix dimer (courtesy of Dr. Axel BrŸnger, Yale). One of the two central Gly-Val motifs is shown as space-filling models. Note how the two glycines pack across the helix-helix interface, and how the flanking valines cover the Gly-Gly contact area.

Figure 10

Model for the phospholamban pentameric ion channel viewed from outside the membrane (PDB file 1PSL). All leucine residues are shown as space-filling models.

Figure 11

Topogenic signals in membrane proteins. SP = signal peptide cleaved by signal peptidase (Lep in E. coli), ST = stop-transfer sequence, SA = signal-anchor sequence, rSA = reverse signal-anchor sequence. Note that all topogenic signals consist of a hydrophobic segment flanked on its cytoplasmic side by positively charged residues.


Arne Elofsson
Last modified: Mon Oct 12 13:45:24 CEST 2001
Arne Elofsson
Stockholm Bioinformatics Center,
Department of Biochemistry,
Arrheniuslaboratoriet
Stockholms Universitet
10691 Stockholm, Sweden
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