Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble.

ABSTRACT: To explore how distal mutations affect binding sites and how binding sites in proteins communicate, an ensemble-based model of the native state was used to define the energetic connectivities between the different structural elements of Escherichia coli dihydrofolate reductase. Analysis of this model protein has allowed us to identify two important aspects of intramolecular communication. First, within a protein, pair-wise couplings exist that define the magnitude and extent to which mutational effects propagate from the point of origin. These pair-wise couplings can be identified from a quantity we define as the residue-specific connectivity. Second, in addition to the pair-wise energetic coupling between residues, there exists functional connectivity, which identifies energetic coupling

SUBMITTER: Pan H 

PROVIDER: S-EPMC17287 | biostudies-literature | 2000 Oct

REPOSITORIES: biostudies-literature