Conformational Selection Governs Carrier Domain Positioning in Staphylococcus aureus Pyruvate Carboxylase.

ABSTRACT: Biotin-dependent enzymes employ a carrier domain to efficiently transport reaction intermediates between distant active sites. The translocation of this carrier domain is critical to the interpretation of kinetic and structural studies, but there have been few direct attempts to investigate the dynamic interplay between ligand binding and carrier domain positioning in biotin-dependent enzymes. Pyruvate carboxylase (PC) catalyzes the MgATP-dependent carboxylation of pyruvate where the biotinylated carrier domain must translocate ∼70 Å from the biotin carboxylase domain to the carboxyltransferase domain. Many prior studies have assumed that carrier domain movement is governed by ligand-induced conformational changes, but the mechanism underlying this movement has not been confirmed. Here, we

SUBMITTER: Hakala JH 

PROVIDER: S-EPMC11451948 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature