Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey.

By András Szilágyi, Péter Závodszky. Structure, 2000

652 citations recorded by the source corpus.

BACKGROUND Proteins from thermophilic organisms usually show high intrinsic thermal stability but have structures that are very similar to their mesophilic homologues. From prevous studies it is difficult to draw general conclusions about the structural features underlying the increased thermal stability of thermophilic proteins. RESULTS In order to reveal the general evolutionary strategy for changing the heat stability of proteins, a non-redundant data set was compiled comprising all high-quality structures of thermophilic proteins and their mesophilic homologues from the Protein Data Bank. The selection (quality) criteria were met by 64 mesophilic and 29 thermophilic protein subunits, representing 25 protein families. From the atomic coordinates, 13 structural parameters were calculated, compared and evaluated using statistical methods. This study is distinguished from earlier ones by the strict quality control of the structures used and the size of the data set. CONCLUSIONS Different protein families adapt to higher temperatures by different sets of structural devices. Regarding the structural parameters, the only generally observed rule is an increase in the number of ion pairs with increasing growth temperature. Other parameters show just a trend, whereas the number of hydrogen bonds and the polarity of buried surfaces exhibit no clear-cut tendency to change with growth temperature. Proteins from extreme thermophiles are stabilized in different ways to moderately thermophilic ones. The preferences of these two groups are different with regards to the number of ion pairs, the number of cavities, the polarity of exposed surface and the secondary structural composition.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/1d217aaee69127863ebff027329c27d61844b3d1

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Citations in the corpus

Thermophilic Adaptation of Proteins (2001, background): “Szilagyi and Závodszky (2000) generated a nonredundant data set containing all available high-quality X-ray structures of monomers and subunits of thermophilic proteins and their mesophilic counterparts.”
Protein and DNA Sequence Determinants of Thermophilic Adaptation (2006, background): “range them into sequences that fold into unique native structures [1] [2] [3] [4]. Indeed, it is well known that enhanced thermostability is reflected in the specific trends in amino acid composition [5] [6] [7]. The most pronounced trends are a elevated fraction of charged residues [8] [9] [10] [11”