Changes in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family members.

ABSTRACT: Oligomerization is a functional requirement for many proteins. The interfacial interactions and the overall packing geometry of the individual monomers are viewed as important determinants of the thermodynamic stability and allosteric regulation of oligomers. The present study focuses on the role of the interfacial interactions and overall contact topology in the dynamic features acquired in the oligomeric state. To this aim, the collective dynamics of enzymes belonging to the amino acid kinase family both in dimeric and hexameric forms are examined by means of an elastic network model, and the softest collective motions (i.e., lowest frequency or global modes of motions) favored by the overall architecture are analyzed. Notably, the lowest-frequency modes accessible to the individual subu

SUBMITTER: Marcos E 

PROVIDER: S-EPMC3182869 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature