[en] Methanothermus fervidus belongs to the group of hyperthermophilic Archaea. The Archaea comprise organisms that live under environmental extremes. like high temperature, low pH value or high salt concentration. The outer surface of the pseudomurein sacculi of the cells of Methanothermus fervidus is covered by glycoprotein subunits (S-Iayer) directly exposed to the extreme environment. The elucidation of the crystal structure of this surface glycoprotein may provide important information on the survival strategies of these unusual micro-organisms. Before our investigations neither three-dimensional crystals have been obtained nor X-ray analyses were performed. Only electron microscopic and computer image enhancement techniques have been applied to obtain structural information from crystalline two-dimensional S-layer sheets. We describe here the successful crystallization of this surface glycoprotein under microgravity conditions.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Evrard, Christine ; Université Catholique de Louvain - UCL > Département de Chimie > Laboratoire de Chimie Physique et de Cristallographie
Declercq, Jean-Paul; Université Catholique de Louvain - UCL > Département de chimie > Laboratoire de Chimie Physique et de Cristallographie
Debaerdemaeker, Tony; Universität Ulm
König, Helmut; Johannes Gutenberg Universität, Mainz
Language :
English
Title :
The first successful crystallization of a prokaryotic extremely thermophilic outer surface layer glycoprotein
Balch, W. E.; Fox, G. E.; Magrum, L. J.; Woese, C. R.; Wolfe, R. S.: Methanogens: Reevaluation of a unique biological group. Microbiol. Rev. 43 (1979) 260-296.
Bosch, R.; Lautenschlager, P.; Potthast, L.; Stapelmann, J.: Experiment equipment for protein crystallization in μg facilities. J. Cryst. Growth. 122 (1992) 310-316.
Bröckl, G.; Behr, M.; Fabry, S.; Hensel, R.; Kaudewitz, H.; Biendl, E.; König, H.: Analysis and nucleotide sequence of the genes encoding the surface-layer glycoproteins of the hyperthermophilic methanogens Methanothermus fervidus and Methanothermus sociabilis. Eur. J. Biochem. 199 (1991) 147-152.
Declercq, J. P.; Evrard, C.; Carter, D. C.; Wright, B. S.; Etienne, G.; Parello, J.: A crystal of a typical EF-hand protein grown under microgravity diffracts X-rays beyond 0.9 Å resolution. J. Cryst. Growth. 196 (1999) 595-601.
Esposito, L.; Sica, F.; Sorrentino, G.; Berisio, R.; Carotenuto, L.; Giordano, A.; Raia, C. A.; Rossi, M.; Lamzin, V. S.; Wilson, K. S.; Zagari, A.: Protein crystal growth in the advanced protein crystallization facility on the LMS mission: a comparison of Sufolobus solfataricus alcohol dehydrogenase crystals grown on the ground and in microgravity. Acta Crystallogr. D54 (1998) 386-390.
Jänicke, R.: Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202 (1991) 715-728.
Jaenicke, R.; Böhm, G.: The stability of proteins in extreme environments. Curr. Opin. Struct. Biol. 8 (1998) 738-748.
Kandler, O.; König, H.: Cell envelopes of archaebacteria. In: The Bacteria. A Treatise on Structure and Function. Vol. VIII. Archaebacteria. (Eds. C. R. Woese, R. S. Wolfe), p. 413-457. Academic Press. New York 1985.
Kandler, O.; König, H.: Cell envelopes of Archaea: structure and chemistry. In: The Biochemistry of Archaea (Archaebacteria). (Eds. H. Kates, D. J. Kushner, A. T. Matheson). p. 223-259. Elsevier Science Publishers, Amsterdam 1993.
Kärcher, U.; Schröder, H.; Haslinger, E.; Allmaier, G.; Schreiner, R.; Wieland, F.; Haselbeck, A.; König, H.: Primary structure of the heterosaccharide of the surface glycoprotein of Methanothermus fervidus. J. Biol. Chem. 268 (1993) 26821-26826.
König, H. ; Messner, P. (Eds.): International Workshop on Structure, Biochemistry, Molecular Biology and Applications of Microbial S-Layers. Special Issue. FEMS Microbiol. (1997) Rev. 20: Vol. 1 + 2.
Laemmli, U.K. : Cleavage of structural proteins during tha assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685.
Lauerer, G.; Kristjansson, J. K.; Langworthy, T. A.; König, H.; Stetter, K. O.: Methanothermus sociabilis sp. nov., a second species within the Methanothermaceae growing at 97°C. System. Appl. Microbiol. 8 (1986) 100-105.
Matthews, B. W.: Solvent content in protein crystals. J. Mol. Biol. 33 (1968) 491-497.
Messner, P. ; Sleytr, U. B.: Crystalline bacterial cell surface layers. In: Advances in Microbial Physiology (Ed. A. H. Rose). Vol. 33, p. 213-275. Academic Press, London 1992.
Nußer, E.; Hartmann, E.; Allmeier, H.; König, H.; Paul, G.; Stetter, K.O.: A glycoprotein surface layer covers the pseudomurein sacculus of the extreme thermophile Methanothermus fervidus. In: Crystalline Bacterial Cell Surface Layers (Eds. U. B. Sleytr, P. Messner, D. Pum, M. Sára), p. 21-25, Springer Verlag, Berlin 1988.
Otwinowsky, Z.; Minor, W.: Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326.
Sleytr, U. B.; Bayley, H.; Sára, M.; Breitwieser, A.; Küpkü, S.; Mader, C.; Weigert, S.; Unger, F. M.; Messner, P.; Jahn-Schmid, B.; Schuster, B.; Pum, D.; Douglas, K.; Clark, N. A.; Moore, J. T.; Winningham, T. A.; Levy, S.; Frithsen, I.; Pankovc, J.; Beale, P.; Gillis, H. P.; Choutov, D. A.; Martin, K. P.: Application of S-layers. FEMS Microbiology Reviews. 20 (1997) 151-175.
Snell, E. H.; Weisberger, S.; Helliwell, J. R.: Improvements in lysozyme protein crystal perfection through microgravity growth. Acta Crystallogr. D51 (1995) 1099-1102.
Stetter, K. O.; Thomm, M.; Winter, J.; Wildgruber, G.; Huber, H.; Zillig, W.; Janecovic, D.; König, H.; Palm, P.; Wunderl, S.: Methanothermus fervidus, sp. nov., a novel extremely thermophilic methanogen isolated from an Icelandic hot sprins. Zbl. Bakt. Hyg., I. Abt. Orig. C. 2 (1981) 166-178.
Wardell, M. R.; Skinner, R.; Carter, D. C.; Twigg, P. D.; Abrahams, J.-P.: Improved diffraction of antithrombin crystals grown in microgravity. Acta Crystallogr. D53 (1997) 622-625.
Woese, C. R.; Kandler, O.; Wheelis, M. L.: Towards a natural system of organisms: proposal for the domains Archaea, Bacteria and Eucarya. Proc. Natl. Acad. Sci. USA 87 (1990) 4576-4579.
