A flexible, allosteric loop regulates protein activity and rewires electrostatics.

ABSTRACT: Allostery is a key driver of protein function and behavior in biological systems. Historically, allosteric regulation has been attributed to conformational and dynamic changes, mostly derived from well-structured regions of proteins. While the regulatory contributions of specific unstructured elements, such as catalytic loops near the active site, have been widely characterized, the role of distal, flexible loops remains poorly understood. Here, we investigate the allosteric protein chorismate mutase (CM), a homodimeric enzyme critical for the biosynthesis of aromatic amino acids. Although CM is differentially regulated by tryptophan and tyrosine via a shared pocket over 25 Å from the active site, their near-identical NMR spectra suggest that alternative mechanisms may explain TrpCM and Ty

SUBMITTER: Vera-Rodriguez DJ 

PROVIDER: S-EPMC12459221 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature