Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1996 Jun;178(11):3025–3030. doi: 10.1128/jb.178.11.3025-3030.1996

Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans monitored by atomic force microscopy.

D J Müller 1, W Baumeister 1, A Engel 1
PMCID: PMC178047  PMID: 8655475

Abstract

Both surfaces of the hexagonally packed intermediate (HPI) layer of Deinococcus radiodurans were imaged in buffer solution by atomic force microscopy. When adsorbed to freshly cleaved mica, the hydrophilic outer surface of the HPI layer was attached to the substrate and the hydrophobic inner surface was exposed to the stylus. The height of a single HPI layer was 7.0 nm, while overlapping edges of adjacent single layers adsorbed to mica had a height of 14.7 nm. However, double-layered stacks with inner surfaces facing each other exhibited a height of 17.4 nm. These stacks exposed the outer surface to the stylus. The different heights of overlapping layers and stacks are attributed to differences in the interaction between inner and outer surfaces. At high resolution, the inner surface revealed a protruding core with a central pore connected by six emanating arms. The pores exhibited two conformations, one with and the other without a central plug. Individual pores were observed to switch from one state to the other.

Full Text

The Full Text of this article is available as a PDF (1.1 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baumeister W., Barth M., Hegerl R., Guckenberger R., Hahn M., Saxton W. O. Three-dimensional structure of the regular surface layer (HPI layer) of Deinococcus radiodurans. J Mol Biol. 1986 Jan 20;187(2):241–250. doi: 10.1016/0022-2836(86)90231-7. [DOI] [PubMed] [Google Scholar]
  2. Baumeister W., Karrenberg F., Rachel R., Engel A., ten Heggeler B., Saxton W. O. The major cell envelope protein of Micrococcus radiodurans (R1). Structural and chemical characterization. Eur J Biochem. 1982 Jul;125(3):535–544. doi: 10.1111/j.1432-1033.1982.tb06715.x. [DOI] [PubMed] [Google Scholar]
  3. Baumeister W., Wildhaber I., Engelhardt H. Bacterial surface proteins. Some structural, functional and evolutionary aspects. Biophys Chem. 1988 Feb;29(1-2):39–49. doi: 10.1016/0301-4622(88)87023-6. [DOI] [PubMed] [Google Scholar]
  4. Baumeister W., Wildhaber I., Phipps B. M. Principles of organization in eubacterial and archaebacterial surface proteins. Can J Microbiol. 1989 Jan;35(1):215–227. doi: 10.1139/m89-034. [DOI] [PubMed] [Google Scholar]
  5. Beveridge T. J. Ultrastructure, chemistry, and function of the bacterial wall. Int Rev Cytol. 1981;72:229–317. doi: 10.1016/s0074-7696(08)61198-5. [DOI] [PubMed] [Google Scholar]
  6. Binnig G, Quate CF, Gerber C. Atomic force microscope. Phys Rev Lett. 1986 Mar 3;56(9):930–933. doi: 10.1103/PhysRevLett.56.930. [DOI] [PubMed] [Google Scholar]
  7. Butt H. J., Downing K. H., Hansma P. K. Imaging the membrane protein bacteriorhodopsin with the atomic force microscope. Biophys J. 1990 Dec;58(6):1473–1480. doi: 10.1016/S0006-3495(90)82492-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Drake B., Prater C. B., Weisenhorn A. L., Gould S. A., Albrecht T. R., Quate C. F., Cannell D. S., Hansma H. G., Hansma P. K. Imaging crystals, polymers, and processes in water with the atomic force microscope. Science. 1989 Mar 24;243(4898):1586–1589. doi: 10.1126/science.2928794. [DOI] [PubMed] [Google Scholar]
  9. Engel A., Baumeister W., Saxton W. O. Mass mapping of a protein complex with the scanning transmission electron microscope. Proc Natl Acad Sci U S A. 1982 Jul;79(13):4050–4054. doi: 10.1073/pnas.79.13.4050. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Frank J., Bretaudiere J. P., Carazo J. M., Verschoor A., Wagenknecht T. Classification of images of biomolecular assemblies: a study of ribosomes and ribosomal subunits of Escherichia coli. J Microsc. 1988 May;150(Pt 2):99–115. doi: 10.1111/j.1365-2818.1988.tb04602.x. [DOI] [PubMed] [Google Scholar]
  11. Hoh J. H., Sosinsky G. E., Revel J. P., Hansma P. K. Structure of the extracellular surface of the gap junction by atomic force microscopy. Biophys J. 1993 Jul;65(1):149–163. doi: 10.1016/S0006-3495(93)81074-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Karrasch S., Dolder M., Schabert F., Ramsden J., Engel A. Covalent binding of biological samples to solid supports for scanning probe microscopy in buffer solution. Biophys J. 1993 Dec;65(6):2437–2446. doi: 10.1016/S0006-3495(93)81327-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Karrasch S., Hegerl R., Hoh J. H., Baumeister W., Engel A. Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment. Proc Natl Acad Sci U S A. 1994 Feb 1;91(3):836–838. doi: 10.1073/pnas.91.3.836. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kellenberger E., Häner M., Wurtz M. The wrapping phenomenon in air-dried and negatively stained preparations. Ultramicroscopy. 1982;9(1-2):139–150. doi: 10.1016/0304-3991(82)90236-4. [DOI] [PubMed] [Google Scholar]
  15. Müller D. J., Büldt G., Engel A. Force-induced conformational change of bacteriorhodopsin. J Mol Biol. 1995 Jun 2;249(2):239–243. doi: 10.1006/jmbi.1995.0292. [DOI] [PubMed] [Google Scholar]
  16. Müller D. J., Schabert F. A., Büldt G., Engel A. Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy. Biophys J. 1995 May;68(5):1681–1686. doi: 10.1016/S0006-3495(95)80345-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Peters J., Peters M., Lottspeich F., Schäfer W., Baumeister W. Nucleotide sequence analysis of the gene encoding the Deinococcus radiodurans surface protein, derived amino acid sequence, and complementary protein chemical studies. J Bacteriol. 1987 Nov;169(11):5216–5223. doi: 10.1128/jb.169.11.5216-5223.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Schabert F. A., Henn C., Engel A. Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy. Science. 1995 Apr 7;268(5207):92–94. doi: 10.1126/science.7701347. [DOI] [PubMed] [Google Scholar]
  19. Sleytr U. B., Messner P. Crystalline surface layers in procaryotes. J Bacteriol. 1988 Jul;170(7):2891–2897. doi: 10.1128/jb.170.7.2891-2897.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sleytr U. B., Messner P. Crystalline surface layers on bacteria. Annu Rev Microbiol. 1983;37:311–339. doi: 10.1146/annurev.mi.37.100183.001523. [DOI] [PubMed] [Google Scholar]
  21. Stemmer A., Reichelt R., Wyss R., Engel A. Biological structures imaged in a hybrid scanning transmission electron microscope and scanning tunneling microscope. Ultramicroscopy. 1991 Jun;35(3-4):255–264. doi: 10.1016/0304-3991(91)90077-j. [DOI] [PubMed] [Google Scholar]
  22. Wang Z. H., Hartmann T., Baumeister W., Guckenberger R. Thickness determination of biological samples with a zeta-calibrated scanning tunneling microscope. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9343–9347. doi: 10.1073/pnas.87.23.9343. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Yang J., Mou J., Shao Z. Molecular resolution atomic force microscopy of soluble proteins in solution. Biochim Biophys Acta. 1994 Mar 2;1199(2):105–114. doi: 10.1016/0304-4165(94)90104-x. [DOI] [PubMed] [Google Scholar]
  24. van Heel M. Multivariate statistical classification of noisy images (randomly oriented biological macromolecules). Ultramicroscopy. 1984;13(1-2):165–183. doi: 10.1016/0304-3991(84)90066-4. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES