pH-dependent interactions guide the folding and gate the transmembrane pore of the β-barrel membrane protein OmpG

Journal of Molecular Biology

Volumn 397, Issue 4, 2010, Pages 878-882

  Damaghi, Mehdi ^a,b   Bippes, Christian ^a,b   Köster, Stefan ^c   Yildiz, Özkan ^c   Mari, Stefania A ^a,b   Kühlbrandt, Werner ^c   Muller, Daniel J ^a,b  

^a DRESDEN UNIVERSITY OF TECHNOLOGY   (Germany)

^b ETH ZURICH   (Switzerland)

^c MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

Author keywords

Escherichia coli; Molecular interactions; PH gating; Unfolding; barrel membrane protein

Indexed keywords

MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN G; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; CHANNEL GATING; CONTROLLED STUDY; ESCHERICHIA COLI; MOLECULAR INTERACTION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; QUANTITATIVE ANALYSIS;

ESCHERICHIA COLI;

EID: 77950021500     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.02.023     Document Type: Article

References (17)

1. Schulz G. Bacterial porins: structure and function. Curr. Opin. Cell Biol. 1993, 5:701-707.
2. Schulz G.E. The structure of bacterial outer membrane proteins. Biochim. Biophys. Acta 2002, 1565:308-317.
3. Yildiz O., Vinothkumar K.R., Goswami P., Kühlbrandt W. Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation. EMBO J. 2006, 25:3702-3713.
4. Subbarao G.V., van den Berg B. Crystal structure of the monomeric porin OmpG. J. Mol. Biol. 2006, 360:750-759.
5. Conlan S., Zhang Y., Cheley S., Bayley H. Biochemical and biophysical characterization of OmpG: a monomeric porin. Biochemistry 2000, 39:11845-11854.
6. Mari S.A., Koster S., Bippes C., Yildiz O., Kühlbrandt W., Muller D.J. pH-induced conformational change of the beta-barrel forming protein OmpG reconstituted into native E. coli lipids. J. Mol. Biol. 2010, 396:610-616.
7. Muller D.J., Engel A. Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy. J. Mol. Biol. 1999, 285:1347-1351.
8. Andersen C., Schiffler B., Charbit A., Benz R. pH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding. J. Biol. Chem. 2002, 277:41318-41325.
9. Kedrov A., Janovjak H., Sapra K.T., Muller D.J. Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy. Annu. Rev. Biophys. Biomol. Struct. 2007, 36:233-260.
10. Engel A., Gaub H.E. Structure and mechanics of membrane proteins. Annu. Rev. Biochem. 2008, 77:127-148.
11. Sapra K.T., Damaghi M., Koester S., Yildiz O., Kühlbrandt W., Muller D.J. One b hairpin after the other: exploring mechanical unfolding pathways of the transmembrane β-barrel protein OmpG. Angew. Chem. Int. Ed. 2009, 48:8306-8308.
12. Muller D.J., Engel A. Atomic force microscopy and spectroscopy of native membrane proteins. Nat. Protoc. 2007, 2:2191-2197.
13. Butt H.-J., Jaschke M. Calculation of thermal noise in atomic force microscopy. Nanotechnology 1995, 6:1-7.
14. Muller D.J., Kessler M., Oesterhelt F., Moeller C., Oesterhelt D., Gaub H. Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy. Biophys. J. 2002, 83:3578-3588.
15. Oesterhelt F., Oesterhelt D., Pfeiffer M., Engel A., Gaub H.E., Muller D.J. Unfolding pathways of individual bacteriorhodopsins. Science 2000, 288:143-146.
16. Kedrov A., Ziegler C., Janovjak H., Kühlbrandt W., Muller D.J. Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy. J. Mol. Biol. 2004, 340:1143-1152.
17. Muller D.J., Engel A., Matthey U., Meier T., Dimroth P., Suda K. Observing membrane protein diffusion at subnanometer resolution. J. Mol. Biol. 2003, 327:925-930.