Locating ligand binding and activation of a single antiporter

EMBO Reports

Volumn 6, Issue 7, 2005, Pages 668-674

  Kedrov, Alexej ^a   Krieg, Michael ^a   Ziegler, Christine ^b   Kuhlbrandt, Werner ^b   Muller, Daniel J ^a  

^a DRESDEN UNIVERSITY OF TECHNOLOGY   (Germany)

^b MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

Author keywords

Atomic force microscopy; Molecular interactions; NhaA; pH activation

Indexed keywords

SODIUM ION; SODIUM PROTON EXCHANGE PROTEIN;

ARTICLE; ATOMIC FORCE MICROSCOPY; BINDING SITE; CONTROLLED STUDY; FORCE; LIGAND BINDING; MOLECULAR INTERACTION; PH; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; STATISTICAL ANALYSIS; STRENGTH;

AMINO ACID SEQUENCE; BINDING SITES; CELL MEMBRANE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROGEN-ION CONCENTRATION; LIGANDS; MICROSCOPY, ATOMIC FORCE; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SODIUM; SODIUM-HYDROGEN ANTIPORTER;

EID: 23744506838     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.embor.7400455     Document Type: Article

References (33)

1. Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, Iwata S (2003) Structure and mechanism of the lactose permease of Escherichia coli. Science 301: 610-615
2. Abramson J, Iwata S, Kaback HR (2004) Lactose permease as a paradigm for membrane transport proteins. Mol Membr Biol 21: 227-236
3. Albrecht C, Blank K, Lalic-Multhaler M, Hirler S, Mai T, Gilbert I, Schiffman S, Bayer T, Clausen-Schaumann H, Gaub HE (2003) DNA: a programmable force sensor. Science 301: 367-370
4. Bustamante C, Siggia ED, Smith S (1994) Entropic elasticity of λ-phage DNA. Science 265: 1599-1600
5. Butt HJ (1995) Calculation of thermal noise in atomic force microscopy. Nanotechnology 6: 1-7
6. Cisneros D, Oesterhelt D, Muller DJ (2005) Probing origins of molecular interactions stabilizing the membrane proteins halorodopsin and bacteriorhodopsin. Structure 13: 235-242
7. Ferguson AD, Chakraborty R, Smith BS, Esser L, Helm D, Deisenhofer J (2002) Structural basis of gating by the outer membrane transporter FecA. Science 295: 1715-1719
8. Florin EL, Rief M, Lehmann H, Ludwig M, Dornmair C, Moy VT, Gaub HE (1995) Sensing specific molecular interactions with the atomic force microscopy. Biosens Bioelectron 10: 895-901
9. Galili L, Rothman A, Kozachkov L, Rimon A, Padan E (2002) Trans membrane domain IV is involved in ion transport activity and pH regulation of the NhaA-Na(+)/H(+) antiporter of Escherichia coli. Biochemistry 41: 609-617
10. + antiporter of Escherichia coli. J Biol Chem 279: 23104-23113
11. + antiporter in Escherichia coli. Proc Natl Acad Sci USA 90: 1212-1216
12. Gerchman Y, Rimon A, Padan E (1999) A pH-dependent conformational change of NhaA Na(+)/H(+) 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
13. + antiporter (NhaA) from Escherichia coli. FEBS Lett 363: 264-268
14. Janovjak H, Kessler M, Oesterhelt D, Gaub H, Muller DJ (2003) Unfolding pathways of native bacteriorhodopsin depend on temperature. EMBO J 22: 5220-5229
15. Janovjak H, Struckmeier J, Hubain M, Kedrov A, Kessler M, Muller DJ (2004) Probing the energy landscape of the membrane protein bacteriorhodopsin. Structure 12: 871-879
16. Karmazyn M, Gan XT, Humphreys RA, Yoshida H, Kusumoto K (1999) The myocardial Na(+)-H(+) exchange: structure, regulation, and its role in heart disease. Circ Res 85: 777-786
17. Kedrov A, Ziegler C, Janovjak H, Kuhlbrandt W, Muller DJ (2004) Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy. J Mol Biol 340: 1143-1152
18. +/galactose cotransporter. Biochemistry 41: 8082-8086
19. Moller C, Fotiadis D, Suda K, Engel A, Kessler M, Muller DJ (2003) Determining molecular forces that stabilize human aquaporin-1. J Struct Biol 142: 369-378
20. Muller DJ, Kessler M, Oesterhelt F, Moller C, Oesterhelt D, Gaub H (2002) Stability of bacteriorhodopsin α-helices and loops analyzed by single-molecule force spectroscopy. Biophys J 83: 3578-3588
21. Oesterhelt F, Oesterhelt D, Pfeiffer M, Engel A, Gaub HE, Muller DJ (2000) Unfolding pathways of individual bacteriorhodopsins. Science 288: 143-146
22. Padan E, Venturi M, Gerchman Y, Dover N (2001) Na(+)/H(+) antiporters. Biochim Biophys Acta 1505: 144-157
23. + antiporter as well as the growth phenotype of Escherichia coli. J Biol Chem 273: 26470-26476
24. + antiporter from Escherichia coli. J Biol Chem 271: 32288-32292
25. + antiporter from Escherichia coli, with trypsin. Biochemistry 36: 14572-14576
26. + antiporter coded by nhaA (ant) from Escherichia coli. J Biol Chem 266: 11289-11294
27. + antiporter of Escherichia coli. J Biol Chem 279: 3265-3272
28. Venturi M, Rimon A, Gerchman Y, Hunte C, Padan E, Michel H (2000) The monoclonal antibody 1F6 identifies a pH-dependent conformational change in the hydrophilic NH(2) terminus of NhaA Na(+)/H(+) antiporter of Escherichia coli. J Biol Chem 275: 4734-4742
29. + exchangers. Physiol Rev 77: 51-74
30. Wang Q, Matsushita K, de Foresta B, le Maire M, Kaback HR (1997) Ligand-induced movement of helix X in the lactose permease from E. coli: a fluorescence quenching study. Biochemistry 36: 14120-14127
31. Williams KA (2000) Three-dimensional structure of the ion-coupled transport protein NhaA. Nature 403: 112-115
32. Williams KA, Geldmacher-Kaufer U, Padan E, Schuldiner S, Kuhlbrandt W (1999) Projection structure of NhaA, a secondary transporter from Escherichia coli, at 4.0 Å resolution. EMBO J 18: 3558-3563
33. Zhang W, Guan L, Kaback HR (2002) Helices VII and X in the lactose permease of Escherichia coli: proximity and ligand-induced distance changes. J Mol Biol 315: 53-62