Summary for 1ANF
| Entry DOI | 10.2210/pdb1anf/pdb |
| Related PRD ID | PRD_900001 |
| Descriptor | MALTODEXTRIN-BINDING PROTEIN, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total) |
| Functional Keywords | periplasmic binding protein, sugar transport |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 41095.45 |
| Authors | Spurlino, J.C.,Quiocho, F.A. (deposition date: 1997-06-25, release date: 1997-12-24, Last modification date: 2024-05-22) |
| Primary citation | Quiocho, F.A.,Spurlino, J.C.,Rodseth, L.E. Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor. Structure, 5:997-1015, 1997 Cited by PubMed Abstract: Active-transport processes perform a vital function in the life of a cell, maintaining cell homeostasis and allowing access of nutrients. Maltodextrin/maltose-binding protein (MBP; M(r) = 40k) is a receptor protein which serves as an initial high-affinity binding component of the active-transport system of maltooligosaccharides in bacteria. MBP also participates in chemotaxis towards maltooligosaccharides. The interaction between MBP and specific cytoplasmic membrane proteins initiates either active transport or chemotaxis. In order to gain new understanding of the function of MBP, especially its versatility in binding different linear and cyclic oligosaccharides with similar affinities, we have undertaken high-resolution X-ray analysis of three oligosaccharide-bound structures. PubMed: 9309217DOI: 10.1016/S0969-2126(97)00253-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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