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Literature summary for 2.7.2.3 extracted from

  • Balog, E.; Laberge, M.; Fidy, J.
    The influence of interdomain interactions on the intradomain motions in yeast phosphoglycerate kinase: a molecular dynamics study (2007), Biophys. J., 92, 1709-1716.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
additional information importance of interdomain contacts in the overall dynamics of the protein, 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 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P00560
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Synonyms

Synonyms Comment Organism
PGK
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Saccharomyces cerevisiae