Distinct allosteric pathways in imidazole glycerol phosphate synthase from yeast and bacteria.

ABSTRACT: Understanding the relationship between protein structures and their function is still an open question that becomes very challenging when allostery plays an important functional role. Allosteric proteins, in fact, exploit different ranges of motions (from sidechain local fluctuations to long-range collective motions) to effectively couple distant binding sites, and of particular interest is whether allosteric proteins of the same families with similar functions and structures also necessarily share the same allosteric mechanisms. Here, we compared the early dynamics initiating the allosteric communication of a prototypical allosteric enzyme from two different organisms, i.e., the imidazole glycerol phosphate synthase (IGPS) enzymes from the thermophilic bacteria and the yeast, working at h

SUBMITTER: Maschietto F 

PROVIDER: S-EPMC8758406 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature