Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH

Nature

Volumn 435, Issue 7046, 2005, Pages 1197-1202

  Hunte, Carola ^a   Screpanti, Emanuela ^a   Venturi, Miro ^a   Rimon, Abraham ^b   Padan, Etana ^b   Michel, Hartmut ^a  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^b HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CONCENTRATION (PROCESS); ION EXCHANGE; MUSCLE; PH EFFECTS; PLANTS (BOTANY); POSITIVE IONS; SALINITY MEASUREMENT;

ANTIPORTERS; CELL VOLUME; ELECTRIC IMBALANCE; ION-EXCHANGE MACHINERY;

ELECTRONIC STRUCTURE;

LITHIUM ION; POTASSIUM ION; PROTEIN NHAA; PROTON; SELENOMETHIONINE; SODIUM ION; SODIUM PROTON EXCHANGE PROTEIN; UNCLASSIFIED DRUG;

CELLS AND CELL COMPONENTS; PH;

ADAPTATION; ARTICLE; BINDING SITE; CELL MEMBRANE; CELL PH; CELL VIABILITY; CELL VOLUME; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYTOPLASM; ENTEROBACTERIACEAE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; PROTON SODIUM EXCHANGE; SALINITY; SODIUM CELL LEVEL; X RAY DIFFRACTION;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; ESCHERICHIA COLI PROTEINS; HYDROGEN; HYDROGEN-ION CONCENTRATION; ION TRANSPORT; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTONS; SODIUM; SODIUM-HYDROGEN ANTIPORTER; STRUCTURE-ACTIVITY RELATIONSHIP;

ENTEROBACTERIA; ESCHERICHIA COLI;

EID: 21744436321     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03692     Document Type: Article

References (50)

1. West, I. & Mitchell, P. Proton/sodium ion antiport in Escherichia coil. Biochem. J. 144, 87-90 (1974).
2. + antiporters. Biochim. Biophys. Acta 1505, 144-157 (2001).
3. Orlowski, J. & Grinstein, S. Diversity of the mammalian sodium/proton exchanger SLC9 gene family. Pflugers Arch. 447, 549-565 (2004).
4. + exchangers. J. Biol. Chem. 275, 1-4 (2000).
5. + exchange prevents hypertrophy, fibrosis, and heart failure in β1-adrenergic receptor transgenic mice. Circ. Res. 90, 814-819 (2002).
6. Myers, M. L. in The Sodium-Hydrogen Exchange, from Molecule to its Role in Disease (eds Karmazyn, N., Avkiran, M. & Fliegel, L.) 279-290 (Kluwer Academic, Boston, Massachusetts, 2003)
7. + antiporter. Plant J. 36, 229-239 (2003).
8. + exchange activity in the plasma membrane of Arabidopsis. Plant Physiol. 132, 1041-1052 (2003).
9. + antiport in Arabidopsis. Science 285, 1256-1258 (1999).
10. +- dependence of alkaliphily in Bacillus. Biochim. Biophys. Acta 1505, 158-168 (2001).
11. Hase, C. C. & Mekalanos, J. J. Effects of changes in membrane sodium flux on virulence gene expression in Vibrio cholerae. Proc. Natl Acad. Sci. USA 96, 3183-3187 (1999).
12. + antiporter. Biochim. Biophys. Acta 1658, 2-13 (2004).
13. + antiporter coded by nhaA (ant) from Escherichia coli. J. Biol. Chem. 266, 11289-11294 (1991).
14. + exchanger, NHE1: structure, regulation and cellular actions. Annu. Rev. Pharmacol. Toxicol. 42, 527-552 (2002).
15. Wakabayashi, S., Pang, T., Hisamitsu, T. & Shigekawa, M. in The Sodium-Hydrogen Exchange, from Molecule to its Role in Disease (eds Karmazyn, N., Avkiran, M. & Fliegel, L.) 35-49 (Kluwer Academic, Boston, Massachusetts, 2003).
16. + antiporter of Escherichia coli involves loop VIII-IX, plays a role in the pH response of the protein, and is maintained by the pure protein in dodecyl maltoside. J. Biol. Chem. 274, 24617-24624 (1999).
17. + antiporter of Escherichia coli in the membrane and its functional and structural consequences. Biochemistry 40, 3403-3412 (2001).
18. Williams, K. A., Geldmacher-Kaufer, U., Padan, E., Schuldiner, S. & Kuhlbrandt, W. Projection structure of NhaA, a secondary transporter from Escherichia coli, at 4.0 Å resolution. EMBO J. 18, 3558-3563 (1999).
19. Williams, K. A. Three-dimensional structure of the ion-coupled transport protein NhaA. Nature 403, 112-115 (2000).
20. + antiporter from Escherichia coli. J. Biol. Chem. 271, 32288-32292 (1996).
21. Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T. & MacKinnon, R. X-ray structure of a CIC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature 415, 287-294 (2002).
22. Palsdottir, H. & Hunte, C. Lipids in membrane protein structures. Biochim. Biophys. Acta 1666, 2-18 (2004).
23. Fu, D. et al. Structure of a glycerol-conducting channel and the basis for its selectivity. Science 290, 481-486 (2000).
24. Khademi, S. et al. Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 Å. Science 305, 1587-1594 (2004).
25. von Heijne, G. Membrane protein structure prediction: hydrophobicity analysis and the 'positive inside' rule. J. Mol. Biol. 225, 487-494 (1992).
26. Glusker, J. P. Structural aspects of metal liganding to functional groups in proteins. Adv. Protein Chem. 42, 1-76 (1991).
27. Harding, M. M. The architecture of metal coordination groups in proteins. Acta Crystallogr. D Biol. Crystallogr. 60, 849-859 (2004).
28. + antiporter (NhaA) from Escherichia coli. FEBS Lett. 363, 264-268 (1995).
29. + antiporter of Escherichia coli. Biochemistry 41, 609-617 (2002).
30. + antiporter of Escherichia coli as determined by site-directed thiol cross-linking. Biochemistry 41, 14897-14905 (2002).
31. + antiporter of Escherichia coli. J. Biol. Chem. 279, 3265-3272 (2004).
32. + antiporter of Escherichia coli. J. Biol. Chem. 275, 4734-4742 (2000).
33. Zilberstein, D., Agmon, V., Schuldiner, S. & Padan, E. The sodium/proton antiporter is part of the pH homeostasis mechanism in Escherichia coli. J. Biol. Chem. 257, 3687-3691 (1982).
34. + antiporters: characterization of multiple catalytic modes and a mutagenesis approach to differences in their efflux substrate and coupling ion preferences. J. Bacteriol. 184, 4722-4732 (2002)
35. Jencks, W. P. The utilization of binding energy in coupled vectorial processes. Adv. Enzymol. 51, 75-106 (1980).
36. West, I. C. Ligand conduction and the gated-pore mechanism of transmembrane transport. Biochim. Biophys. Acta 1331, 213-234 (1997).
37. Taglicht, D., Padan, E. & Schuldiner, S. Proton-sodium stoichiometry of NhaA, an electrogenic antiporter from Escherichia coli. J. Biol. Chem. 268, 5382-5387 (1993).
38. + antiporter of Escherichia coli. J. Biol. Chem. 279, 23104-23113 (2004).
39. + antiporter as well as the growth phenotype of Escherichia coli J. Biol. Chem. 273, 26470-26476 (1998).
40. + exchanger. Annu. Rev. Physiol. 47, 545-560 (1985).
41. + exchangers by measurement of reverse mode reaction. J. Biol. Chem. 278, 43580-43585 (2003).
42. Murakami, S., Nakashima, R., Yamashita, E. & Yamaguchi, A. Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419, 587-593 (2002).
43. Abramson, J. et al. Structure and mechanism of the lactose permease of Escherichia coli. Science 301, 610-615 (2003).
44. Pebay-Peyroula, E. et al. Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside. Nature 426, 39-44 (2003).
45. Huang, Y., Lemieux, M. J., Song, J., Auer, M. & Wang, D. N. Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301, 616-620 (2003).
46. Viitanen, P., Garcia, M. L. & Kaback, H. R. Purified reconstituted lac carrier protein from Escherichia coli is fully functional. Proc. Natl Acad. Sci. USA 81, 1629-1633 (1984).
47. Klingenberg, M. in The ADP/ATP Carrier in Mitochondrial Membranes (ed. Martonosi, A. N.) (Plenum, New York, 1985).
48. Auer, M. et al. High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter. Biochemistry 40, 6628-6635 (2001).
49. Liang, J., Edelsbrunner, H. & Woodward, C. Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design. Protein Sci. 7, 1884-1897 (1998).
50. Kleywegt, G. J. & Jones, T. A. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr. D Biol. Crystallogr. 50, 178-185 (1994).