Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel

Nature

Volumn 457, Issue 7225, 2009, Pages 115-118

  Hilf, Ricarda J C ^a   Dutzler, Raimund ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ANION; CATION; ION CHANNEL; PROTEIN; PROTON;

BACTERIUM; CYANOBACTERIUM; FUNDAMENTAL PARTICLE; ION; LIGAND; PH; PROTEIN; THERMODYNAMICS;

ARTICLE; CHANNEL GATING; CONFORMATION; CYANOBACTERIUM; CYTOARCHITECTURE; DIFFUSION; GLOEBACTER VIOLACEUS; HYDROPHOBICITY; LIGAND BINDING; LIPID BILAYER; NONHUMAN; PH; PRIORITY JOURNAL; STRUCTURE ANALYSIS; THERMODYNAMICS; VESTIBULE; X RAY ANALYSIS;

ERWINIA CHRYSANTHEMI; PROKARYOTA;

EID: 58149242730     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature07461     Document Type: Article

References (42)

1. Hilf , R. J. & Dutzler, R. X-ray structure of a prokaryotic pentameric ligand-gated ion channel. Nature 452, 375-379 (2008).
2. Bocquet, N. et al. A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family. Nature 445, 116-119 (2007).
3. Karlin, A. Emerging structure of the nicotinic acetylcholine receptors. Nature Rev. Neurosci. 3, 102-114 (2002).
4. Adams, D. J., Dwyer, T. M. & Hille, B. The permeability of endplate channels to monovalent and divalent metal cations. J. Gen. Physiol. 75, 493-510 (1980).
5. Tasneem, A., Iyer, L. M., Jakobsson, E. & Aravind, L. Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels. Genome Biol. 6, R4 (2004).
6. Miyazawa, A., Fujiyoshi, Y. & Unwin, N. Structure and gating mechanism of the acetylcholine receptor pore. Nature 423, 949-955 (2003).
7. Unwin, N. Refined structure of the nicotinic acetylcholine receptor at 4A° resolution. J. Mol. Biol. 346, 967-989 (2005).
8. Imoto, K. et al. Rings of negatively charged amino acids determine the acetylcholine receptor channel conductance. Nature 335, 645-648 (1988).
9. Konno, T. et al. Rings of anionic amino acids as structural determinants of ion selectivity in the acetylcholine receptor channel. Proc. R. Soc. Lond. B 244, 69-79 (1991).
10. + channel-Fab complex at 2.0 A° resolution. Nature 414, 43-48 (2001).
11. Sine, S. M. & Engel, A. G. Recent advances in Cys-loop receptor structure and function. Nature 440, 448-455 (2006).
12. Brejc, K. et al. Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature 411, 269-276 (2001).
13. Celie, P. H. et al. Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures. Neuron 41, 907-914 (2004).
14. Lee, W. Y. & Sine, S. M. Principal pathway coupling agonist binding to channel gating in nicotinic receptors. Nature 438, 243-247 (2005).
15. Sala, F., Mulet, J., Sala, S., Gerber, S. & Criado, M. Charged amino acids of the N-terminal domain are involved in coupling binding and gating in alpha7 nicotinic receptors. J. Biol. Chem. 280, 6642-6647 (2005).
16. Schofield, C. M., Jenkins, A. & Harrison, N. L. A highly conserved aspartic acid residue in the signature disulfide loop of the alpha 1 subunit is a determinant of gating in the glycine receptor. J. Biol. Chem. 278, 34079-34083 (2003).
17. Jha, A., Cadugan, D. J., Purohit, P. & Auerbach, A. Acetylcholine receptor gating at extracellular transmembrane domain interface: The cys-loop and M2-M3 linker. J. Gen. Physiol. 130, 547-558 (2007).
18. Dani, J. A. Open channel structure and ion binding sites of the nicotinic acetylcholine receptor channel. J. Neurosci. 9, 884-892 (1989).
19. Dani, J. A. & Eisenman, G. Monovalent and divalent cation permeation in acetylcholine receptor channels. Ion transport related to structure. J. Gen. Physiol. 89, 959-983 (1987).
20. Galzi, J. L. et al. Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic. Nature 359, 500-505 (1992).
21. 7 nicotinic acetylcholine receptor. Neuron 22, 831-843 (1999).
22. Gunthorpe, M. J. & Lummis, S. C. Conversion of the ion selectivity of the 5-HT(3a) receptor from cationic to anionic reveals a conserved feature of the ligand-gated ion channel superfamily. J. Biol. Chem. 276, 10977-10983 (2001).
23. Pascual, J. M. & Karlin, A. State-dependent accessibility and electrostatic potential in the channel of the acetylcholine receptor. Inferences from rates of reaction of thiosulfonates with substituted cysteines in the M2 segment of the alpha subunit. J. Gen. Physiol. 111, 717-739 (1998).
24. Wilson, G. G., Pascual, J. M., Brooijmans, N., Murray, D. & Karlin, A. The intrinsic electrostatic potential and the intermediate ring of charge in the acetylcholine receptor channel. J. Gen. Physiol. 115, 93-106 (2000).
25. Unwin, N. Acetylcholine receptor channel imaged in the open state. Nature 373, 37-43 (1995).
26. Paas, Y. et al. Pore conformations and gating mechanism of a Cys-loop receptor. Proc. Natl Acad. Sci. USA 102, 15877-15882 (2005).
27. Cymes, G. D., Ni, Y. & Grosman, C. Probing ion-channel pores one proton at a time. Nature 438, 975-980 (2005).
28. Cymes, G. D. & Grosman, C. Pore-opening mechanism of the nicotinic acetylcholine receptor evinced by proton transfer. Nature Struct. Mol. Biol. 15, 389-396 (2008).
29. Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800 (1993).
30. Leslie, A. G. Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography (No. 26, Daresbury Laboratory, 1992).
31. Evans, P. Scaling and assessment of data quality. Acta Crystallogr. D 62, 72-82 (2006).
32. CCP4. Collaborative Computational Project Nr. 4. The CCP4 Suite: Programs for X-ray crystallography. Acta Crystallogr. D 50, 760-763 (1994).
33. McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
34. Cowtan, K. An automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography 34-38 (No. 31, Daresbury Laboratory, 1994).
35. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
36. Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
37. Adams, P. D. et al. PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948-1954 (2002).
38. Smart, O. S., Neduvelil, J. G., Wang, X., Wallace, B. A. & Sansom, M. S. HOLE: A program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graph. 14, 354-360, 376 (1996).
39. Sanner, M. F., Olson, A. J. & Spehner, J. C. Reduced surface: An efficient way to compute molecular surfaces. Biopolymers 38, 305-320 (1996).
40. Brooks, B. R. et al. CHARMM: A program for macromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 4, 187-217 (1983).
41. Im, W., Beglov, D. & Roux, B. Continuum solvation model: Electrostatic forces from numerical solutions to the Poisson-Boltzmann equation. Comput. Phys. Commun. 111, 59-75 (1998).
42. Lorenz, C., Pusch, M. & Jentsch, T. J. Heteromultimeric CLC chloride channels with novel properties. Proc. Natl Acad. Sci. USA 93, 13362-13366 (1996).