Allostery and cooperativity in multimeric proteins: bond-to-bond propensities in ATCase.

ABSTRACT: Aspartate carbamoyltransferase (ATCase) is a large dodecameric enzyme with six active sites that exhibits allostery: its catalytic rate is modulated by the binding of various substrates at distal points from the active sites. A recently developed method, bond-to-bond propensity analysis, has proven capable of predicting allosteric sites in a wide range of proteins using an energy-weighted atomistic graph obtained from the protein structure and given knowledge only of the location of the active site. Bond-to-bond propensity establishes if energy fluctuations at given bonds have significant effects on any other bond in the protein, by considering their propagation through the protein graph. In this work, we use bond-to-bond propensity analysis to study different aspects of ATCase activity us

SUBMITTER: Hodges M 

PROVIDER: S-EPMC6056424 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature