Study of the influence of temperature on the dynamics of the catalytic cleft in 1,3-1,4-β-glucanase by molecular dynamics simulations

Raimundo Gargallo, Juan Cedano, Angel Mozo-Villarias, Enrique Querol, Baldomero Oliva

Research output: Contribution to journalArticleResearchpeer-review

4 Citations (Scopus)

Abstract

The dependence of some molecular motions in the enzyme 1,3-1,4-β-glucanase from Bacillus licheniformis on temperature changes and the role of the calcium ion in them were explored. For this purpose, two molecular dynamics simulated trajectories along 4 ns at low (300 K) and high (325 K) temperatures were generated by the GROMOS96 package. Several structural and thermodynamic parameters were calculated, including entropy values, solvation energies, and essential dynamics (ED). In addition, thermoinactivation experiments to study the influence of the calcium ion and some residues on the activity were conducted. The results showed the release of the calcium ion, which, in turn, significantly affected the movements of loops 1, 2, and 3, as shown by essential dynamics. These movements differ at low and high temperatures and affect dramatically the activity of the enzyme, as observed by thermoinactivation studies. © Springer-Verlag 2006.
Original languageEnglish
Pages (from-to)835-845
JournalJournal of Molecular Modeling
Volume12
Issue number6
DOIs
Publication statusPublished - 1 Sep 2006

Keywords

  • Enzyme deactivation
  • Essential dynamics
  • Reactionfield
  • Structural alignment
  • Thermoinactivation

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