Crystal structure and functional characterization of OmpK36, the osmoporin of Klebsiella pneumoniae

Structure

Volumn 7, Issue 4, 1999, Pages 425-434

  Dutzler, R ^a   Rummel, G ^b   Alberti, S ^c   Hernandez Alles S ^c   Phale, P S ^b   Rosenbusch, J P ^b   Benedi, V J ^c   Schirmer, T ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b UNIVERSITY OF BASEL   (Switzerland)

^c INSTITUTO MEDITERRÁNEO DE ESTUDIOS AVANZADOS   (Spain)

Author keywords

Electrophysiology; Nonspecific porin; OmpK36; Outer membrane protein; X ray structure

Indexed keywords

MEMBRANE PROTEIN; PORIN;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; GENE DELETION; GENE INSERTION; KLEBSIELLA PNEUMONIAE; LIPID BILAYER; NONHUMAN; OSMOTIC PRESSURE; OUTER MEMBRANE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN ISOLATION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

ESCHERICHIA COLI; KLEBSIELLA PNEUMONIAE; NEGIBACTERIA;

EID: 0033560795     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80055-0     Document Type: Article

References (49)

1. Schirmer, T. (1998). General and specific porins from bacterial outer membranes. J. Struct. Biol. 121, 101-109.
2. Jap, B.K. & Walian, P.J. (1996). Structure and functional mechanism of porins. Physiol. Rev. 76, 1073-1088.
3. Schulz, G.E. (1996). Porins: General to specific, native to engineered passive pores. Can, Opin. Struct. Biol. 6, 485-490.
4. Nikaido, H. (1994). Porins and specific diffusion channels in bacterial outer membranes. J. Biol. Chem. 269, 3905-3908.
5. Nikaido, H. & Rosenberg, E.Y. (1983). Porin channels in Escherichia coli: Studies with liposomes reconstituted from purified protein. J. Bacteriol. 153, 241-252.
6. Mizuno, T., Chou, M.-Y. & Inouye, M. (1983). A comparative study on the genes for three porins of the Escherichia coli outer membrane. DNA sequence of the osmoregulated gene. J. Biol. Chem. 258, 6932-6940.
7. Lugtenberg, B. & Van Alphen, L. (1983). Molecular architecture and functioning of the outer membrane of Escherichia coli and other gram-negative bacteria. Biochim. Biophys. Acta 737, 51-115.
8. Hall, M.N. & Silhavy, T.J. (1981). Genetic analysis of the major outer membrane proteins of Escherichia coli. Ann Rev. Genet. 15, 91-142.
9. Forst, S. & Inouye, M. (1988). Environmentally regulated gene expression for membrane proteins in Escherichia coli. Ann Rev. Cell Biol. 4, 21-42.
10. Pratt, L.A., Hsing, W., Gibson, K.E. & Silhavy, T.J. (1996). From acids to osmZ: Multiple factors influence synthesis of the OmpF and OmpC porins in Escherichia coli. Mol. Microbiol. 20, 911-917.
11. Benz, R., Schmid, A. & Hancock, R.E.W. (1985). Ion selectivity of Gram-negative bacterial porins. J. Bacteriol. 162, 722-727.
12. Lakey, J.H., Watts, J.P. & Lea, E.J. (1985). Characterisation of channels induced in planar bilayer membranes by detergent solubilised Escherichia coli porins. Biochim. Biophys. Acta 817, 208-16.
13. Prilipov, A., Phale, P.S., Koebnik, R., Widmer, C. & Rosenbusch, J.P. (1998). Identification and characterization of two quiescent porin genes, nmpC and ompN, in Escherichia coli BE. J. Bacteriol. 180, 3388-3392.
14. Buehler, L.K., Kusumoto, S., Zhang, H. & Rosenbusch, J.P. (1991). Plasticity of Escherichia coli porin channels. Dependence of their conductance on strain and lipid environment. J. Biol. Chem. 266, 24446-24450.
15. Weiss, M.S., Abele, U., Weckesser, J., Welte, W., Schiltz, E. & Shulz, G.E. (1991). Molecular architecture and electrostatic properties of a bacterial porin. Science 254, 1627-1630.
16. Cowan, S.W., et al., & Rosenbusch, J.P. (1992). Crystal structures explain functional properties of two E. coli porins. Nature 358, 727-733.
17. Kreusch, A., Neubüser, E., Schiltz, E., Weckesser, J. & Schulz, G.E. (1994). Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution. Protein Sci. 3, 58-63.
18. Karshikoff, A., Spassov, V., Cowan, S.A., Ladenstein, R. & Schirmer, T. (1994). Electrostatic properties of two porin channels from E.coli. J. Mol. Biol. 240, 372-384.
19. Alberti, S., Rodriguez-Quinones, F., Schirmer, T., Rummel, G., Rosenbusch, J.P. & Benedi, V.J. (1995). A porin from Klebsiella pneumoniae: Sequence homology, three-dimensional model, and complement binding. Infect. Immun. 63, 903-910.
20. Benedi, V.J., Vivanco, F. & Tomás, J. (1998). Complement activation in Klebsiella pneumoniae. Rev. Med. Microbiol. 9, 69-77.
21. Alberti, S., Benedi, V.J. & et al., (1993). C1q binding and activation of the complement classical pathway by Klebsiella pneumoniae outer membrane proteins. Infect. Immun. 61, 852-860.
22. Michel, H. (1983). Crystallization of membrane proteins. Trends Biochem Sci., 56-59.
23. Phale, P.S., et al., & Rosenbuch, J.P. (1998). Stability of trimeric OmpF porin: The contributions of the latching loop L2. Biochemistry 37, 15663-15670.
24. Duncan, A.R. & Winter, G. (1988). The binding site for C1q on IgG. Nature 332, 738-740.
25. Deisenhofer, J. (1981). Crystallographic refinement and atomic models of a human Fc Fragment B of Protein A from Staphylococcus aureus at 2.9 and 2.8 Å resolution. Biochemistry 20, 2361-2370.
26. Ebenbichler, C.F., Thielens, N.M., Vornhagen, R., Marschang, P., Arlaud, G.J. & Dierich, M.P. (1991). Human immunodeficiency virus type 1 activates the classical pathway of complement by direct C1 binding through specific sites in the transmembrane glycoprotein gp41. J. Exp. Med. 174, 1417-1424.
27. Madura, J.D., McCammon, J.A. & et al., (1995). Electrostatics and diffusion in solution: Simulations with the University of Huston Brownian Dynamics Program. Comp. Phys. Commun. 91, 57-95.
28. Hille, B. (1992). Ionic Channels of Excitable Membranes. Sinauer Associates Inc., Sunderland, MA.
29. Hodgkin, A.L. & Katz, B. (1949). The effect of sodium ions on the electrical activity of the giant axon of the squid. J. Physiol. 108, 37-77.
30. Nikaido, H., Rosenberg, E.Y. & Foulds, J. (1983). Porin channels in Escherichia coli: Studies with β-lactams in intact cells. J. Bacteriol. 153, 232-240.
31. Harder, K.J., Nikaido, H. & Matsuhashi, M. (1981). Mutants of Escherichia coli that are resistant to certain beta-lactam compounds lack the OmpF porin. Antimicrob. Agents Chemother. 20, 549-52.
32. Benz, R. (1985). Porin from bacterial and mitochondrial outer membranes. CRC Crit. Rev. Biochem. 19, 145-190.
33. Chen, D. & Eisenberg, R. (1993). Charges, currents, and potentials in ionic channels of one conformation. Biophys. J. 64, 1405-1421.
34. Brunen, M., Engelhardt, H., Schmid, A. & Benz, R. (1991). The major outer membrane protein of Acidovorax delafieldii is an anion-selective porin. J. Bacteriol. 173, 4182-7.
35. Chen, D., Lear, J. & Eisenberg, B. (1997). Permeation trough an open channel: Poisson-Nernst-Planck theory of a synthetic ionic channel. Biophys. J. 72, 97-116.
36. Dutzler, R. (1998). Structural Studies on Solute Transport Through Transmembrane Channel Proteins. PhD thesis, University of Basel, Basel, Switzerland.
37. Sen, K., Hellman, J. and Nikaido, H. (1988). Porin channels in intact cells of Escherichia coli are not affected by Donnan potentials across the outer membrane. J. Biol. Chem. 263, 1182-1187.
38. Delcour, A.H. (1997). Function and modulation of bacterial porins: Insights from electrophysiology. FEMS Microbiol. Lett. 151, 115-123.
39. Saint, N., Lou, K.-L., Widmer, C., Luckey, M., Schirmer, T. & Rosenbusch, J.P. (1996). Structural and functional characterization of OmpF porin mutants selected for larger pore size. II. Functional characterization. J. Biol. Chem. 271, 20676-20680.
40. Leslie, A.G.W. (1992). In Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography, no. 26. SERC Daresbury Laboratory, Warrington, U.K.
41. Collaborative computational project, number 4 (1994). The CCP4 suite: Programs for protein crystallography. Acta. Cryst. D 50, 760-763.
42. Navaza, J. (1994). AMoRe: An automated package for molecular replacement. Acta Cryst. A 50, 157-163.
43. Cowtan, K.D. & Main, P. (1996). Phase combination and cross validation in iterated density-modification calculations. Acta. Cryst. D 52, 43-48.
44. Jones, T.A. & Kjeldgaard, M., O Version 5.9, The Manual (Upsala University, Upsala, Sweden, 1993).
45. Brünger, A.T (1992). X-PLOR Version 3.1. A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT.
46. Jiang, J.-S. & Brünger, A.T. (1994). Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243, 100-115.
47. Jorgensen, W. & Tirado-Rives, J. (1988). The OPLS potential function for proteins, energy minimization for crystals of cyclic peptides and crambin. J. Am. Chem. Soc. 110, 1657-1666.
48. Esterling, L. & Delihas, N. (1994). The regulatory RNA gene micF is present in several species of Gram-negative bacteria and is phylogenetically conserved. Mol. Microbiol. 12, 639-46.
49. Sanner, M.F., Olson, A.J. & Spehner, J.C. (1996). Reduced surface: An efficient way to compute molecular surfaces. Biopolymers 38, 305-20.