Ontology highlight
ABSTRACT:
SUBMITTER: Lisi GP
PROVIDER: S-EPMC4938718 | biostudies-literature | 2016 Jul
REPOSITORIES: biostudies-literature
Lisi George P GP Manley Gregory A GA Hendrickson Heidi H Rivalta Ivan I Batista Victor S VS Loria J Patrick JP
Structure (London, England : 1993) 20160526 7
The allosteric mechanism of the heterodimeric enzyme imidazole glycerol phosphate synthase was studied in detail with solution nuclear magnetic resonance spectroscopy and molecular dynamics simulations. We studied IGPS in complex with a series of allosteric activators corresponding to a large range of catalytic rate enhancements (26- to 4,900-fold), in which ligand binding is entropically driven. Conformational flexibility on the millisecond timescale plays a crucial role in intersubunit communi ...[more]