Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers

Protein Science

Volumn 7, Issue 2, 1998, Pages 342-348

  Kim, Yongae ^a,c   Valentine, Kathleen ^a   Opella, Stanley J ^a   Schendel, Sharon L ^b,d   Cramer, William A ^b  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b PURDUE UNIVERSITY   (United States)

^c LG Chemical Ltd   (South Korea)

^d BURNHAM INSTITUTE   (United States)

Author keywords

Colicin, ion channel; Membrane proteins; Membranes; Protein import; Solid state NMR; Voltage gated channel

Indexed keywords

COLICIN E1;

ARTICLE; LIPID BILAYER; MEMBRANE BINDING; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; SOLID STATE; STRUCTURE ACTIVITY RELATION;

EID: 0031891529     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070214     Document Type: Article

References (43)

1. Anraku Y. 1967. The reduction and restoration of galactose transport in osmotically shocked cells of Escherichia coli. J Biol Chem 242:793-800.
2. Bechinger B, Gierasch LM, Montal M, Zasloff M, Opella SJ. 1996. Orientations of helical peptides in membrane bilayers by solid-state NMR spectroscopy. Solid-state NMK 7:185-191.
3. Bechinger B, Kim Y, Chirlian LE, Gesell J, Neumann JM, Montal M, Tomich J, Zasloff M, Opella SJ, 1991 Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy. J Biomolec NMR 1:167-173.
4. Braun V, Pilsl H. 1995. Novel colicin 10: Assignment of four domains to TonB and TolC-dependent uptake via the Tsx receptor and pore formation. Mol Microbiol 16:57-67.
5. Bullock JO, Cohen FS, Dankert JR, Cramer WA. 1983. Comparison of the macroscopic and single channel conductance properties of colicin E1 and its COOH-terminal tryptic peptide. J Biol Chem 258:9908-9912.
6. Cleveland MV, Slatin S, Finkelstein A, Levinthal C. 1983. Structure-function relationships for a voltage-dependent ion channel: Properties of COOH-terminal fragments of colicin E1. Proc Natl Acad Sci USA 80:3706-3710.
7. Cramer WA, Heymann JB, Schendel SL, Deriy BN, Cohen FS, Elkins PA, Stauffacher CV. 1995. Structure-function of the channel-forming colicins. Annu Rev Biophys Biomol Struct 24:611-641.
8. Cross TA, Opella SJ. 1994. Solid-state NMR structural studies of peptides and proteins in membranes. Curr Opin Struct Biol 4:572-581.
9. Dankert JR, Uratani Y, Grabau C, Cramer WA, Hermodson M. 1982. On a domain structure of colicin E1: A COOH-terminal peptide fragment active in membrane depolarization. J Biol Chem 257:3857-3863.
10. Duché D, Parker MW, González-Mañas, Pattus F, Baty D. 1994. Uncoupled steps of the colicin A pore formation demonstrated by disulfide engineering. J Biol Chem 269:6332-6339.
11. Elkins P, Song HY, Cramer WA, Stauffacher CV. 1994. Crystallization and characterization of colicin E1 channel-forming polypeptides. Proteins Struct Funct Genet 19:150-157.
12. Elkins P, Bunker A, Cramer WA, Stauffacher CV. 1997. The crystal structure of the channel-forming domain of colicin E1. Structure 5:443-458.
13. Geli V, Koorengevel MC, Demel RA. 1992. Acidic interaction of the colicin A pore-forming domain with model membranes of Escherichia coli lipids results in a large perturbation of acyl chain order and stabilization of the bilayer. Biochemistry 31:11089-11094.
14. Gonzalez-Mañas JM, Lakey JH, Pattus F. 1992. Brominated phospholipids as a tool for monitoring the membrane insertion of colicin A. Biochemistry 31:7294-7300.
15. Goormaghtigh E, Vigneron L, Knibiehler M, Lazdunski C, Ruysschaert JM. 1991. Secondary structure of the membrane-bound form of the pore-forming domain of colicin A. Eur J Biochem 202:1299-1305.
16. Gould JM, Cramer WA. 1977. Studies on the depolarization of the Escherichia coli cell membrane by colicin E1. J Biol Chem 252:5491-5497.
17. Heymann JB, Zakharov SD, Zhang Y-L, Cramer WA. 1996. Characterization of electrostatic and non-electrostatic protein-membrane binding interactions. Biochemistry 35:2717-2725.
18. Jeanteur D, Pattus F. 1994. Membrane-bound form of the pore-forming domain of colicin A. J Mol Biol 235:898-907.
19. a hydrophobic hairpin. J Memb Biol 157:27-37.
20. Lakey JH, Duché D, González-Manas J-M. 1993. Fluorescence energy transfer distance measurements. The hydrophobic helical hairpin of colicin A in the membrane bound state. J Mol Biol 230:1055-1067.
21. 15N-labeled membrane protein in phospholipid bilayers. Proc Natl Acad Sci USA 94:8551-8556.
22. Massotte D, Dasseux J-L, Sauve P, Cyrklaff M, Leonard K, Pattus F. 1989. Interaction of the pore-forming domain of colicin A with phospholipid vesicles. Biochemistry 28:7713-7719.
23. Massotte D, Yamamoto M, Scianimanico S, Sorokine O, van Dorsselaer A, Nakatani Y, Ourisson G, Pattus F. 1993. Structure of the membrane-bound form of the pore-forming domain of colicin A: A partial proteolysis and mass spectrometry study. Biochemistry 32:13787-13794.
24. McDonnell PA, Shon K, Kim Y, Opella SJ. 1993. fd coat protein structure in membrane environments. J Mol Biol 233:447-463.
25. Merrill AR, Cramer WA. 1990. Identification of a voltage-responsive segment of the potential-gated colicin E1 ion channel. Biochemistry 29:8529-8534.
26. Opella SJ, Stewart PL, Valentine KG. 1987. Protein structure by solid-state NMR spectroscopy. Q Rev Biophys 19:7-49.
27. Opella SJ. 1985. Protein dynamics by solid-state NMR. Methods Enzymol 131:327-361.
28. Parker MW, Pattus F. 1993. Rendering a membrane protein soluble in water: A common packing motif in bacterial protein toxins. Trends Biosci 18:391-395.
29. Parker MW, Pattus F, Tucker AD, Tsernoglou D. 1989. Structure of the membrane-pore-forming fragment of colicin A. Nature 337:93-96.
30. Parker MW, Postma JPM, Pattus F, Tucker AD, Tsernoglou D. 1992. Refined structure of the pore-forming domain of colicin A at 2.4 Å resolution. J Mol Biol 224:639-657.
31. Pattus F, Martinez MC, Dargen B, Carvard D, Verger R, Lazdunski C. 1983. Interaction of colicin A with phospholipid monolayers and liposomes. Biochemistry 22:5698-5703.
32. Ramamoorthy A, Marassi FM, Zasloff M, Opella SJ. 1995. Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers. J Biomol NMR 6:329-334.
33. Rath P, Bousché O, Merrill AR, Cramer WA, Rothschild KJ. 1991. Fourier transform infrared evidence for a predominantly α-helical structure of the membrane bound channel forming COOH-terminal peptide of colicin E1. Biophys J 59:516-522.
34. Shibuya I. 1992. Metabolic regulation and biological functions of phospholipids in Escherichia coli. Prog Lipid Res 31:245-299.
35. Shin Y-K, Levinthal C, Levinthal F, Hubbell WL. 1993. Colicin E1 binding to membranes: Time-resolved studies of spin-labeled mutants. Science 259:960-963.
36. Shon K, Kim Y, Colnago L, Opella SJ. 1991. NMR studies of the structure and dynamics of membrane bound bacteriophage Pf1 coat protein. Science 252:1303-1305.
37. Slatin SL, Qiu X-Q, Jakes KS, Finkelstein A. 1994. Identification of a trans-located protein segment in a voltage-dependent channel. Nature 371:158-161.
38. Song HY, Cohen FS, Cramer WA. 1991. Membrane topography of Co1E1 gene products: The hydrophobic anchor of the colicin E1 channel is a helical hairpin. J Bacteriol 173:2927-2934.
39. Wiener MC, Freymann D, Stroud RM, Ghosh P. 1996. Crystal structure of colicin Ia. Nature 385:461-464.
40. Wu CH, Ramamoorthy A, Opella SJ. 1994. High-resolution heteronuclear dipolar solid-state NMR spectroscopy. J Magn Res 109:270-272.
41. Zakharov SD, Heymann JB, Zhang YL, Cramer, WA. 1996. Characterization of membrane binding of the colicin E1 channel domain: Maximum activity is associated with an intermediate strength of the surface electrostatic interaction. Biophys J 70:2774-2783.
42. Zakharov SD, Venyaminov SY, Prendergast FG, Cramer WA. 1997. Structure analysis of the C-terminal channel domain of colicin E1 in its solution and membrane-bound states. Biophys J 72:A230.
43. Zhang Y-L, Cramer WA. 1992. Constraints imposed by protease accessibility on the trans-membrane and surface topography of the colicin E1 ion channel. Protein Sci 1:1666-1676.