2FN8
Thermotoga maritima Ribose Binding Protein Ribose Bound Form
Summary for 2FN8
Entry DOI | 10.2210/pdb2fn8/pdb |
Related | 2FN9 2FNC |
Descriptor | ribose ABC transporter, periplasmic ribose-binding protein, beta-D-ribopyranose (3 entities in total) |
Functional Keywords | rbp, ribose binding protein, periplasmic binding protein, thermophilic protein, sugar binding protein |
Biological source | Thermotoga maritima |
Total number of polymer chains | 1 |
Total formula weight | 33984.38 |
Authors | Cuneo, M.J.,Changela, A. (deposition date: 2006-01-10, release date: 2007-01-16, Last modification date: 2023-09-20) |
Primary citation | Cuneo, M.J.,Beese, L.S.,Hellinga, H.W. Ligand-induced conformational changes in a thermophilic ribose-binding protein. Bmc Struct.Biol., 8:50-50, 2008 Cited by 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. PubMed: 19019243DOI: 10.1186/1472-6807-8-50 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
Download full validation report