Lipid-protein interactions probed by electron crystallography

Current Opinion in Structural Biology

Volumn 19, Issue 5, 2009, Pages 560-565

  Reichow, Steve L ^a   Gonen, Tamir ^a,b  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AQUAPORIN; BACTERIORHODOPSIN; MEMBRANE PROTEIN;

CONTROLLED STUDY; CRYOELECTRON MICROSCOPY; CRYSTALLOGRAPHY; ELECTRON CRYSTALLOGRAPHY; ION TRANSPORT; LIGHT; LIPID BILAYER; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FUNCTION; PROTEIN LIPID INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW; STRUCTURE ANALYSIS;

CRYSTALLOGRAPHY, X-RAY; LIPIDS; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; PROTEINS;

EID: 70349863382     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2009.07.012     Document Type: Review

References (25)

1. Henderson R., and Unwin P.N. Three-dimensional model of purple membrane obtained by electron microscopy. Nature 257 (1975) 28-32
2. Grigorieff N., Ceska T.A., Downing K.H., Baldwin J.M., and Henderson R. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J Mol Biol 259 (1996) 393-421
3. Mitsuoka K., Hirai T., Murata K., Miyazawa A., Kidera A., Kimura Y., and 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. This paper describes the 3 Å resolution electron crystallographic structure of bacteriorhodopsin. Specifically bound lipids are resolved and lipid-protein interactions discussed. Charges on protein amino acid residues are also visualized by electron microscopy.
4. Gonen T., Cheng Y., Sliz P., Hiroaki Y., Fujiyoshi Y., Harrison S., and Walz T. Lipid-protein interactions in double-layered two-dimensional crystals of aquaporin-0. Nature 438 (2005) 633-638. This paper describes the 1.9 Å resolution electron crystallographic structure of aquaporin-0. Nonspecific lipid-protein interactions are described.
5. Subramaniam S., Hirai T., and Henderson R. From structure to mechanism: electron crystallographic studies of bacteriorhodopsin. Philos Trans A Math Phys Eng Sci 360 (2002) 859-874
6. Cartailler J.P., and Luecke H. X-ray crystallographic analysis of lipid-protein interactions in the bacteriorhodopsin purple membrane. Annu Rev Biophys Biomol Struct 32 (2003) 285-310
7. Sternberg B., L'Hostis C., Whiteway C.A., and Watts A. The essential role of specific Halobacterium halobium polar lipids in 2D-array formation of bacteriorhodopsin. Biochim Biophys Acta 1108 (1992) 21-30
8. Hojeberg B., Lind C., and Khorana H.G. Reconstitution of bacteriorhodopsin vesicles with Halobacterium halobium lipids. Effects of variations in lipid composition. J Biol Chem 257 (1982) 1690-1694
9. Ulmschneider M.B., and Sansom M.S. Amino acid distributions in integral membrane protein structures. Biochim Biophys Acta 1512 (2001) 1-14
10. Andrews S., Reichow S.L., and Gonen T. Electron crystallography of aquaporins. IUBMB Life 60 (2008) 430-436
11. Gonen T., and Walz T. The structure of aquaporins. Q Rev Biophys 39 (2006) 361-396. This is a thorough review on aquaporin structures determined both by electron and X-ray crystallography.
12. Reichow S.L., and Gonen T. Noncanonical binding of calmodulin to aquaporin-0: implications for channel regulation. Structure 16 (2008) 1389-1398. Oligomerization in aquaporins is important for the binding of regulatory proteins such as calmodulin.
13. Preston G.M., Carroll T.P., Guggino W.B., and Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256 (1992) 385-387
14. Zeidel M.L., Ambudkar S.V., Smith B.L., and Agre P. Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein. Biochemistry 31 (1992) 7436-7440
15. Walz T., Smith B.L., Zeidel M.L., Engel A., and Agre P. Biologically active two-dimensional crystals of aquaporin CHIP. J Biol Chem 269 (1994) 1583-1586
16. Hunte C. Specific protein-lipid interactions in membrane proteins. Biochem Soc Trans 33 (2005) 938-942
17. Hite R.K., Gonen T., Harrison S.C., and Walz T. Interactions of lipids with aquaporin-0 and other membrane proteins. Pflugers Arch (2007). The temperature B-factors of bacteriorhodopsin and aquaporin-0 determined by both electron and X-ray crystallography are systematically compared and contrasted. Special attention is given to amino acid residues that are interacting with lipid or detergent molecules. An overall stabilizing effect of lipids on protein is observed.
18. Clemons Jr. W.M., Menetret J.F., Akey C.W., and Rapoport T.A. Structural insight into the protein translocation channel. Curr Opin Struct Biol 14 (2004) 390-396
19. Appel M., Hizlan D., Vinothkumar K.R., Ziegler C., and Kuhlbrandt W. Conformations of NhaA, the Na/H exchanger from Escherichia coli, in the pH-activated and ion-translocating states. J Mol Biol 386 (2009) 351-365. The ion channel NhaA crystallizes as a monomer in 3D crystals but dimers are physiologically important and indeed 2D crystals contain dimers. This paper suggests that crystallographic protein-protein contacts may inhibit the NhaA transport mechanism.
20. Subramaniam S., Lindahl M., Bullough P., Faruqi A.R., Tittor J., Oesterhelt D., Brown L., Lanyi J., and Henderson R. Protein conformational changes in the bacteriorhodopsin photocycle. J Mol Biol 287 (1999) 145-161
21. Berriman J., and Unwin N. Analysis of transient structures by cryo-microscopy combined with rapid mixing of spray droplets. Ultramicroscopy 56 (1994) 241-252
22. Hunte C., and Richers S. Lipids and membrane protein structures. Curr Opin Struct Biol 18 (2008) 406-411
23. Van den Berg B., Clemons Jr. W.M., Collinson I., Modis Y., Hartmann E., Harrison S.C., and Rapoport T.A. X-ray structure of a protein-conducting channel. Nature 427 (2004) 36-44
24. + antiporter and insights into mechanism of action and regulation by pH. Nature 435 (2005) 1197-1202
25. Osborne A.R., and Rapoport T.A. Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel. Cell 129 (2007) 97-110