Commentary: Membrane protein assemblies - Towards atomic resolution analysis

Current Opinion in Structural Biology

Volumn 10, Issue 2, 2000, Pages 208-212

  Tsukihara, Tomitake ^a   Aoyama, Hiroshi ^b  

^a OSAKA UNIVERSITY   (Japan)

^b INST OF PHYS AND CHEMICAL RESEARCH   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; CYTOCHROME C OXIDASE; MEMBRANE LIPID; MEMBRANE PROTEIN; MEMBRANE RECEPTOR; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UBIQUINOL CYTOCHROME C REDUCTASE; BACTERIAL PROTEIN; PORIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

CELL RESPIRATION; ENZYME STRUCTURE; LIPID ANALYSIS; LIPID BILAYER; MEMBRANE STRUCTURE; NOTE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN FOLDING; X RAY CRYSTALLOGRAPHY; ANIMAL; CHEMISTRY; CRYSTALLIZATION; METHODOLOGY; PROTEIN TERTIARY STRUCTURE; REVIEW;

ANIMALS; BACTERIAL PROTEINS; BACTERIORHODOPSINS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ELECTRON TRANSPORT COMPLEX III; ELECTRON TRANSPORT COMPLEX IV; MEMBRANE LIPIDS; MEMBRANE PROTEINS; PORINS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTON-TRANSLOCATING ATPASES;

EID: 0034168591     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(00)00069-5     Document Type: Review

References (30)

1. Luecke H., Schobert B., Richter H.T., Cartailler J.P., Lanyi J.K. Structure of bacteriorhodopsin at 1.55 Å resolution. J Mol Biol. 291:1999;899-911. The highest resolution structure of a membrane protein is described.
2. Luecke H., Schobert B., Richter H.T., Cartailler J.P., Lanyi J.K. Structure change in bacteriorhodopsin during ion transport at 2 angstrom resolution. Science. 286:1999;255-260. A mechanism of proton translocation based on the structure of a reaction intermediate of bacteriorhodopsin was clearly determined using a mutant protein.
3. Edman K., Nollert P., Royant A., Belrhall H., Pebay-Peyroula E., Hajdu J., Neutze R., Landau E.M. High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle. Nature. 401:1999;822-826. The authors reveal the high-resolution structure of a bacteriorhodopsin intermediate.
4. Iverson T.M., Luna-Chavez C., Cecchini G., Rees D.C. Structure of the Escherichia coli fumarate reductase respiratory complex. Science. 284:1999;1961-1966. The structure of a respiratory complex that is homologous to respiratory complex II is described. The structures of the subunits reveal evolutional relationships with other proteins. The locations of active centers and the electron transfer mechanism are presented.
5. Wendt K.U., Lenhart A., Schulz G.E. The structure of the membrane protein squalene-hopene cyclase at 2. 0 Å resolution. J Mol Biol. 286:1999;175-187.
6. Wendt K.U., Poralla K., Schulz G.E. Structure and function of a squalene cyclase. Science. 277:1997;1811-1815.
7. Banfield M.J., Barker J.J., Perry A.C., Brady R.L. Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure. 6:1998;1245-1254.
8. Olson R., Nariya H., Yokota K., Kamio Y., Gouaux E. Crystal structure of staphylococcal LukF delineates conformational change accompanying formation of a transmembrane channel. Nat Struct Biol. 6:1999;134-140. The structure of a water-soluble monomeric membrane protein was determined. A mechanism of pore formation was proposed by comparing the monomeric structure and an oligomeric pore structure.
9. Pedelacq J.D., Maveyraud L., Prevost G., Baba-Moussa L., Gonzalez A., Courcelle E., Shepard W., Monteil H., Samama J.P., Mourey L. The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins. Structure. 7:1999;277-287. Electron microscopy structures of oligomeric pore-forming toxins were determined. A pore-forming mechanism is proposed.
10. Gilbert R.J.C., Jimenez J.L., Chen S., Tickle I.J., Rossjohn J., Parker M., Andrew P.W., Saibil H.R. Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae. Cell. 97:1999;647-655.
11. Dutzler R., Rummel G., Albert S., Hernandez-Alles S., Phale P.S., Rosenbusch J.P., Benedi V.J., Schirmer T. Crystal structure and functional characterization of OmpK36, the osmoporin of Klebsiella pneumoniae. Structure. 7:1999;425-434.
12. Miyazawa A., Fujiyoshi Y., Stowell M., Unwin N. Nicotinic acetylcholine receptor at 4.6 Å resolution: transverse tunnels in the channel wall. J Mol Biol. 288:1999;765-786. The high-resolution structure of a membrane protein receptor is described.
13. Mitsuoka K., Hirai T., Murata K., Miyazawa A., Kidera A., Kimura Y., Fujiyoshi Y. The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: implication of the charge distribution. J Mol Biol. 286:1999;861-882. A strategy to evaluate charge densities using the electron diffraction method is given.
14. +-ATPase on a carbon support film for electron crystallography. J Mol Biol. 287:1999;961-968.
15. Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H., Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2. 8 Å resolution. Science. 272:1996;1136-1144.
16. Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:1995;660-669.
17. Grigorieff N., Ceska T.A., Downing K.H., Baldwin J.M., Henderson R. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J Mol Biol. 259:1996;393-421.
18. Essen L.O., Siegert R., Lehmann W.D., Oesterhelt D. Lipid patches in membrane protein oligomers. crystal structure of the bacteriorhodopsin-lipid complex Proc Natl Acad Sci USA. 95:1998;11673-11678.
19. Sato H., Takeda K., Tani K., Hino T., Okada T., Nakasako M., Kamiya N., Kouyama T. Specific lipid-protein interactions in a novel honeycomb lattice structure of bacteriorhodopsin. Acta Crystallogr D55. 1999;1251-1256.
20. Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H., Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S. Structure of metal sites of oxidized cytochrome c oxidase at 2.8 Å Science. 269:1995;1069-1074.
21. V fragment. Proc Natl Acad Sci USA. 94:1997;10547-10553.
22. 1 complex from bovine heart mitochondria. Science. 277:1997;60-66.
23. 1. Nature. 392:1998;677-684.
24. 1complex. Science. 280:1998;1934-1937.
25. Toyoshima C., Unwin N. Ion channel of acetylcholine receptor reconstituted from images of postsynaptic membranes. Nature. 336:1988;247-250.
26. Song L., Hobaugh M.R., Shustak C., Cheley S., Bayley H., Gouaux J.E. Structure of staphylococcal α-hemolysin, heptameric transmembrane pore. Science. 274:1996;1859-1866.
27. + conduction and selectivity Science. 280:1998;69-77.
28. + channel β subunit. Cell. 97:1999;943-952.
29. + channel. electrostatic mobilisation of monovalent cations Science. 285:1999;100-102.
30. +-channel activation gating. Science. 285:1999;73-78.