Download MendeleyLigand-induced conformational changes in a thermophilic ribose-binding protein.
Cuneo, M.J., Beese, L.S., Hellinga, H.W.(2008) BMC Struct Biol 8: 50-50
- PubMed: 19019243
- DOI: https://doi.org/10.1186/1472-6807-8-50
- Primary Citation of Related Structures:
2FN9 - PubMed Abstract:
Members of the periplasmic binding protein (PBP) superfamily are involved in transport and signaling processes in both prokaryotes and eukaryotes. Biological responses are typically mediated by ligand-induced conformational changes in which the binding event is coupled to a hinge-bending motion that brings together two domains in a closed form. In all PBP-mediated biological processes, downstream partners recognize the closed form of the protein. This motion has also been exploited in protein engineering experiments to construct biosensors that transduce ligand binding to a variety of physical signals. Understanding the mechanistic details of PBP conformational changes, both global (hinge bending, twisting, shear movements) and local (rotamer changes, backbone motion), therefore is not only important for understanding their biological function but also for protein engineering experiments.
Organizational Affiliation:
The Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA. mjc18@duke.edu
