The influence of interdomain interactions on the intradomain motions in yeast phosphoglycerate kinase: A molecular dynamics study

Erika Balog, Monique Laberge, Judit Fidy

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A 3-ns molecular dynamics simulation in explicit solvent was performed to examine the inter- and intradomain motions of the two-domain enzyme yeast phosphoglycerate kinase without the presence of substrates. To elucidate contributions from individual domains, simulations were carried out on the complete enzyme as well as on each isolated domain. The enzyme is known to undergo a hinge-bending type of motion as it cycles from an open to a closed conformation to allow the phosphoryl transfer occur. Analysis of the correlation of atomic movements during the simulations confirms hinge bending in the nanosecond timescale: the two domains of the complete enzyme exhibit rigid body motions anticorrelated with respect to each other. The correlation of the intradomain motions of both domains converges, yielding a distinct correlation map in the enzyme. In the isolated domain simulations - in which interdomain interactions cannot occur - the correlation of domain motions no longer converges and shows a very small correlation during the same simulation time. This result points to the importance of interdomain contacts in the overall dynamics of the protein. The secondary structure elements responsible for interdomain contacts are also discussed.

Original languageEnglish
Pages (from-to)1709-1716
Number of pages8
JournalBiophysical journal
Issue number5
Publication statusPublished - Mar 2007


ASJC Scopus subject areas

  • Biophysics

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