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2FN9

Thermotoga maritima Ribose Binding Protein Unliganded Form

Summary for 2FN9
Entry DOI10.2210/pdb2fn9/pdb
Related2FN8 2FNC
Descriptorribose ABC transporter, periplasmic ribose-binding protein (2 entities in total)
Functional Keywordsrbp, ribose binding protein, periplasmic binding protein, thermophilic proteins, sugar binding protein
Biological sourceThermotoga maritima
Total number of polymer chains2
Total formula weight64404.86
Authors
Cuneo, M.J.,Changela, A.,Tian, Y.,Beese, L.S.,Hellinga, H.W. (deposition date: 2006-01-10, release date: 2007-01-16, Last modification date: 2023-08-30)
Primary citationCuneo, 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: 19019243
DOI: 10.1186/1472-6807-8-50
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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