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Comparative analysis of thermal adaptations of extremophilic prolyl oligopeptidases.
Diessner, Elizabeth M; Takahashi, Gemma R; Butts, Carter T; Martin, Rachel W.
Afiliación
  • Diessner EM; Department of Chemistry, University of California, Irvine, Irvine, California.
  • Takahashi GR; Department of Molecular Biology & Biochemistry, University of California, Irvine, Irvine, California.
  • Butts CT; Departments of Sociology, Statistics, Computer Science, and EECS, University of California, Irvine, Irvine, California. Electronic address: buttsc@uci.edu.
  • Martin RW; Department of Chemistry, University of California, Irvine, Irvine, California; Department of Molecular Biology & Biochemistry, University of California, Irvine, Irvine, California. Electronic address: rwmartin@uci.edu.
Biophys J ; 2024 Jul 15.
Article en En | MEDLINE | ID: mdl-39014897
ABSTRACT
Prolyl oligopeptidases from psychrophilic, mesophilic, and thermophilic organisms found in a range of natural environments are studied using a combination of protein structure prediction, atomistic molecular dynamics, and trajectory analysis to determine how the S9 protease family adapts to extreme thermal conditions. We compare our results with hypotheses from the literature regarding structural adaptations that allow proteins to maintain structure and function at extreme temperatures, and we find that, in the case of prolyl oligopeptidases, only a subset of proposed adaptations are employed for maintaining stability. The catalytic and propeller domains are highly structured, limiting the range of mutations that can be made to enhance hydrophobicity or form disulfide bonds without disrupting the formation of necessary secondary structure. Rather, we observe a pattern in which overall prevalence of bound interactions (salt bridges and hydrogen bonds) is conserved by using increasing numbers of increasingly short-lived interactions as temperature increases. This suggests a role for an entropic rather than energetic strategy for thermal adaptation in this protein family.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Biophys J Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Biophys J Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos