Hyperthermostable surface layer protein tetrabrachion from the archaebacterium Staphylothermus marinus: Evidence for the presence of a right-handed coiled coil derived from the primary structure

Journal of Molecular Biology

Volumn 257, Issue 5, 1996, Pages 1031-1041

  Peters, Jürgen ^a   Baumeister, Wolfgang ^a   Lupas, Andrei ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Archaebacterial surface protein; Coiled coil; Filamentous; S layer; Thermostable

Indexed keywords

GLYCINE; GLYCOPROTEIN; ISOLEUCINE; LEUCINE; MEMBRANE PROTEIN; PROLINE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARCHAEBACTERIUM; ARTICLE; CARBOXY TERMINAL SEQUENCE; HYDROPHOBICITY; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; THERMOSTABILITY;

ARCHAEA; STAPHYLOTHERMUS MARINUS;

EID: 0029942482     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0221     Document Type: Article

References (25)

1. Baumeister, W. & Engelhardt, H. (1987). Three-dimensional structure of bacterial surface layers. In Electron Microscopy of Proteins, Membranous Structures (Harris, J. R. & Home, R. W., eds.), vol. 6, pp. 109-153, Academic Press, London.
2. Baumeister, W., Wildhaber, I. & Engelhardt, H. (1988). Bacterial surface proteins: some structural, functional and evolutionary aspects. Biophys. Chem. 29, 39-49.
3. Boguski, M. S., Birkenmeier, E. H., Elshourbagy, N. A., Taylor, J. M. & Gordon, J. I. (1986). Evolution of the apolipoproteins. Structure of the rat apo-A-IV gene and its relationship to the human genes for apo-A-I, C-III, and E. J. Biol. Chem. 261, 6398-6407.
4. Breiter, D. R., Kanost, M. R., Benning, M. M., Wesenberg, G., Law, J. H., Wells, M. A., Rayment, I. & Holden, H. (1991). Molecular structure of an apolipoprotein determined at 2.5-Å resolution. Biochemistry, 30, 603-608.
5. Chothia, C. (1984). Principles that determine the structure of proteins. Annu. Rev. Biochem. 53, 537-572.
6. Cohen, C. & Parry, D. A. D. (1990). α-Helical coiled coils and bundles: how to design an α-helical protein. Proteins: Struct. Funct. Genet. 7, 1-15.
7. Crick, F. H. C. (1953a). The Fourier transform of a coiled-coil. Acta Crystallog. 6, 685-689.
8. Crick, F. H. C. (1953b). The packing of α-helices: simple coiled-coils. Acta Crystallog. 6, 689-697.
9. Dure, L., III. (1993). A repeating 11-mer amino acid motif and plant desiccation. Plant J. 3, 363-369.
10. Engel, J. & Furthmayr, H. (1987). Electron microscopy and other physical methods for the characterization of extracellular matrix components: laminin, fibronectin, collagen IV, collagen VI, and proteoglycans. Methods Enzymol. 145, 3-77.
11. Fiala, G., Stetter, K. O., Jannasch, H. W., Langworthy T. A. & Madon, J. (1986). Staphylothermus marinus sp. nov. represents a novel genus of extreme thermophilic submarine heterotrophic archaebacteria growing up to 98°C. System. Appl. Microbiol. 8, 106-113.
12. Fraser, R. D. B. & MacRae, T. P. (1973). Conformation in Fibrous Proteins and Related Synthetic Polypeptides, pp. 456-465, Academic Press, London.
13. Harbury, P. B., Zhang, T., Kim, P. S. & Alber, T. (1993). A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science, 262, 1401-1407.
14. Harbury, P. B., Kim, P. S. & Alber, T. (1994). Crystal structure of an isoleucine-zipper trimer. Nature, 371, 80-83.
15. Lundberg, K. S., Shoemaker, D. D., Adams, M. W. W., Short, J. M. & Mathur, E. J. (1991). High-fidelity amplification using a thermostable DNA polymerase isolated from Pyrococcus furiosus. Gene, 108, 1-6.
16. Lupas, A. (1996). Prediction and analysis of coiled-coil structures. Methods Enzymol., 266, 513-525.
17. Lupas, A., Müller, S., Goldie, K., Engel, A. M., Engel, A. & Baumeister, W. (1995). Model structure of the Ompα rod, a parallel four-stranded coiled coil from the hyperthermophilic eubacterium Thermotoga maritima. J. Mol. Biol. 248, 180-189.
18. Makhov, A. M., Hannah, J. H., Brennan, M. J., Trus, B. L., Kocsis, E., Conway, J. F., Wingfield, P. T., Simon, M. N. & Steven, A. C. (1994). Filamentous hemagglutinin of Bordetella pertussis. J. Mol. Biol. 241, 110-124.
19. Parry, D. A. D. (1987). Fibrous protein structure and sequence analysis. In Fibrous Protein Structure (Squire, J. M. & Vibert, P. J., eds) vol. 6, pp. 141-171, Academic Press, New York.
20. Peters, J., Nitsch, M., Kühlmorgen, B., Golbik, R., Lupas, A., Kellermann, J., Engelhardt, H., Pfander, J. P., Müller, S., Goldie, K., Engel, A., Stetter., K. O. & Baumeister, W. (1995). Tetrabrachion - a filamentous archaebacterial surface protein assembly of unusual structure and extreme stability. J. Mol. Biol. 245, 385-401.
21. Ponder, J. W. & Richards, F. M. (1987). Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193, 775-791.
22. Schägger, H. & Jagow, G. (1987). Tricine-sodium dodecylsulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
23. Sleytr, U. B., Messner, P., Pum, D. & Sara, M. (1993). Crystalline bacterial cell surface layers. Mol. Microbiol. 10, 911-916.
24. Treutlein, H. R., Lemmon, M. A., Engelman, D. M. & Brünger, A. T. (1992). The glycophorin A transmembrane domain dimer: sequence-specific propensity for a right-handed supercoil of helices. Biochemistry, 31, 12726-12733.
25. Wilson, C., Wardell, M. R., Weisgraber, K. H., Mahley R. W. & Agard, D. A. (1991). Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science, 252, 1817-1822.