High stability of the hinge region in the membrane-active peptide helix of zervamicin: Paramagnetic relaxation enhancement studies

Biochemical and Biophysical Research Communications

Volumn 325, Issue 3, 2004, Pages 1099-1105

  Shenkarev, Zakhar O ^a   Paramonov, Alexander S ^a   Balashova, Tamara A ^a   Yakimenko, Zoya A ^a   Baru, Michael B ^b   Mustaeva, Leila G ^b   Raap, Jan ^c   Ovchinnikova, Tatyana V ^a   Arseniev, Alexander S ^a  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^b RUSSIAN ACADEMY OF SCIENCES   (Russian Federation)

^c LEIDEN UNIVERSITY   (Netherlands)

Author keywords

Antibiotic; Channel forming peptide; NMR; Peptaibol

Indexed keywords

AMINO ACID; ION CHANNEL; METHANOL; PEPTAIBOL; PEPTIDE; UNCLASSIFIED DRUG; ZERVAMICIN; ZERVAMICIN 2B;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; AQUEOUS SOLUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CROSS LINKING; ELECTRON SPIN RESONANCE; LIPID BILAYER; MEMBRANE BIOLOGY; MEMBRANE CONDUCTANCE; MICROENVIRONMENT; MOLECULAR INTERACTION; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN STABILITY; REACTION ANALYSIS; STATISTICAL SIGNIFICANCE; STRUCTURE ANALYSIS;

ION CHANNELS; MAGNETIC RESONANCE SPECTROSCOPY; MAGNETICS; MEMBRANE PROTEINS; METHANOL; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SOLUTIONS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 8444250550     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.10.115     Document Type: Article

References (33)

1. H. Duclohier, and H. Wroblewski Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues J. Membr. Biol. 184 2001 1 12
2. L. Beven, O. Helluin, G. Molle, H. Duclohier, and H. Wroblewski Correlation between anti-bacterial activity and pore sizes of two classes of voltage-dependent channel-forming peptides Biochim. Biophys. Acta 1421 1999 53 63
3. 1H NMR. Evidence for conformational heterogeneity in a voltage-gated peptide Biochemistry 33 1994 4036 4045
4. A.A. Yee, R. Babiuk, and J.D. O'Neil The conformation of an alamethicin in methanol by multinuclear NMR-spectroscopy and distance geometry simulated annealing Biopolymers 36 1995 781 792
5. C.L. North, J.C. Franklin, R.G. Bryant, and D.S. Cafiso Molecular flexibility demonstrated by paramagnetic enhancements of nuclear relaxation. Application to alamethicin: a voltage-gated peptide channel Biophys. J. 67 1994 1861 1866
6. J. Jacob, H. Duclohier, and D.S. Cafiso The role of proline and glycine in determining the backbone flexibility of a channel-forming peptide Biophys. J. 76 1999 1367 1376
7. N. Gibbs, R.B. Sessions, P.B. Williams, and C.E. Dempsey Helix bending in alamethicin: molecular dynamics simulations and amide hydrogen exchange in methanol Biophys. J. 72 1997 2490 2495
8. D.P. Tieleman, I.H. Shrivastava, M.R. Ulmschneider, and M.S. Sansom Proline-induced hinges in transmembrane helices: possible roles in ion channel gating Proteins 44 2001 63 72
9. F.S. Cordes, J.N. Bright, and M.S. Sansom Proline-induced distortions of transmembrane helices J. Mol. Biol. 323 2002 951 960
10. S.C. Li, N.K. Goto, K.A. Williams, and C.M. Deber Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environment Proc. Natl. Acad. Sci. USA 93 1996 6676 6681
11. A.D. Argoudelis, A. Dietz, and L.E. Johnson Zervamicins I and II, polypeptide antibiotics produced by Emericellopsis salmosynnemata J. Antibiot. (Tokyo 27 1974 321 328
12. I.L. Karle, J.L. Flippen-Anderson, S. Agarwalla, and P. Balaram Crystal structure of [Leu1]zervamicin, a membrane ion-channel peptide: implications for gating mechanisms Proc. Natl. Acad. Sci. USA 88 1991 5307 5311
13. I.L. Karle, J.L. Flippen-Anderson, S. Agarwalla, and P. Balaram Conformation of the flexible bent helix of Leu1-zervamicin in crystal C and a possible gating action for ion passage Biopolymers 34 1994 721 735
14. T.A. Balashova, Z.O. Shenkarev, A.A. Tagaev, T.V. Ovchinnikova, J. Raap, and A.S. Arseniev NMR structure of the channel-former zervamicin IIB in isotropic solvents FEBS Lett. 466 2000 333 336
15. 15N NMR relaxation FEBS Lett. 495 2001 52 55
16. 15N NMR assignment J. Pept. Sci. 9 2003 817 826
17. Z.O. Shenkarev, T.A. Balashova, R.G. Efremov, Z.A. Yakimenko, T.V. Ovchinnikova, J. Raap, and A.S. Arseniev Spatial structure of zervamicin IIB bound to DPC micelles: implications for voltage-gating Biophys. J. 82 2002 762 771
18. Z.O. Shenkarev, T.A. Balashova, Z.A. Yakimenko, T.V. Ovchinnikova, and A.S. Arseniev Peptaibol zervamicin IIB structure and dynamics refinement from transhydrogen bond J couplings Biophys. J. 86 2004 3687 3699
19. A.D. Milov, Y.D. Tsvetkov, E.Y. Gorbunova, L.G. Mustaeva, T.V. Ovchinnikova, and J. Raap Self-aggregation properties of spin-labeled zervamicin IIA as studied by PELDOR spectroscopy Biopolymers 64 2002 328 336
20. A.S. Altieri, D.P. Hinton, and R.A. Byrd Association of biomolecular systems via pulsed-field gradient NMR self-diffusion measurements J. Am. Chem. Soc. 117 1995 7566 7567
21. R.A. Dwek Nuclear Magnetic Resonance (NMR) in Biochemistry 1973 Clarendon press Oxford
22. P. Guntert, C. Mumenthaler, and K. Wuthrich Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 273 1997 283 298
23. P. Balaram, K. Krishna, M. Sukumar, I.R. Mellor, and M.S. Sansom The properties of ion channels formed by zervamicins Eur. Biophys. J. 21 1992 117 128
24. T. Jin, L. Peng, T. Mirshahi, T. Rohacs, K.W. Chan, R. Sanchez, and D.E. Logothetis The (beta)gamma subunits of G proteins gate a K(+) channel by pivoted bending of a transmembrane segment Mol. Cell 10 2002 469 481
25. Y. Jiang, A. Lee, J. Chen, M. Cadene, B.T. Chait, and R. MacKinnon The open pore conformation of potassium channels Nature 417 2002 523 526
26. R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55 pp. 29-32
27. T.N. Kropacheva, and J. Raap Voltage-dependent interaction of the peptaibol antibiotic zervamicin II with phospholipid vesicles FEBS Lett. 460 1999 500 504
28. 31P solid-state NMR investigations on the orientation of zervamicin II and alamethicin in phosphatidylcholine membranes Biochemistry 40 2001 9428 9437
29. P. Dauber-Osguthorpe, V.A. Roberts, D.J. Osguthorpe, J. Wolff, M. Genest, and A.T. Hagler Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim a drug-receptor system Proteins 4 1988 31 47
30. H. Duclohier, C.F. Snook, and B.A. Wallace Antiamoebin can function as a carrier or as a pore-forming peptaibol Biochim. Biophys. Acta 1415 1998 255 260
31. C.F. Snook, G.A. Woolley, G. Oliva, V. Pattabhi, S.F. Wood, T.L. Blundell, and B.A. Wallace The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide Structure 6 1998 783 792
32. T.P. Galbraith, R. Harris, P.C. Driscoll, and B.A. Wallace Solution NMR studies of antiamoebin, a membrane channel-forming polypeptide Biophys. J. 84 2003 185 194
33. J. Iwahara, C.D. Schwieters, and G.M. Clore Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule J. Am. Chem. Soc. 126 2004 5879 5896