Surface (glyco-)proteins: primary structure and crystallization under microgravity conditions

Details Surface (glyco-)proteins: primary structure and crystallization under microgravity conditions Surface (glyco-)proteins: primary structure and crystallization under microgravity conditions

Aug 2001

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2001esasp.496..313c&link_type=abstract

In: Exo-/astro-biology. Proceedings of the First European Workshop, 21 - 23 May 2001, ESRIN, Frascati, Italy. Eds.: P. Ehrenfreu

Biology

1

Microorganisms

Scientific paper

The Archaea comprise microorganisms that live under environmental extremes, like high temperature, low pH value or high salt concentration. Their cells are often covered by a single layer of (glyco)protein subunits (S-layer) in hexagonal arrangement. In order to get further hints about the molecular mechanisms of protein stabilization we compared the primary and secondary structures of archaeal S-layer (glyco)proteins. We found an increase of charged amino acids in the S-layer proteins of the extreme thermophilic species compared to their mesophilic counterparts. Our data and those of other authors suggest that ionic interactions, e.g., salt bridges seem to be played a major role in protein stabilization at high temperatures. Despite the differences in the growth optima and the predominance of some amino acids the primary structures of S-layers revealed also a significant degree of identity between phylogenetically related archaea. These obervations indicate that protein sequences of S-layers have been conserved during the evolution from extremely thermophilic to mesophilic life. To support these findings the three-dimensional structure of the S-layer proteins has to be elucidated. Recently, we described the first successful crystallization of an extreme thermophilic surface(glyco)protein under microgravity conditions.

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