3PGF
Crystal structure of maltose bound MBP with a conformationally specific synthetic antigen binder (sAB)
Summary for 3PGF
| Entry DOI | 10.2210/pdb3pgf/pdb |
| Related PRD ID | PRD_900001 |
| Descriptor | Maltose-binding periplasmic protein, SAB Heavy Chain, SAB Light Chain, ... (7 entities in total) |
| Functional Keywords | maltodextrin binding protein, fab, antibody fragment, engineered binding protein, maltodextrin binding protein-de novo protein complex, maltodextrin binding protein/de novo protein |
| Biological source | Escherichia coli More |
| Cellular location | Periplasm: P0AEX9 Secreted : P0DOX5 |
| Total number of polymer chains | 3 |
| Total formula weight | 92840.60 |
| Authors | Kossiakoff, A.A.,Duguid, E.M.,Sandstrom, A. (deposition date: 2010-11-01, release date: 2011-03-09, Last modification date: 2024-11-06) |
| Primary citation | Rizk, S.S.,Paduch, M.,Heithaus, J.H.,Duguid, E.M.,Sandstrom, A.,Kossiakoff, A.A. Allosteric control of ligand-binding affinity using engineered conformation-specific effector proteins. Nat.Struct.Mol.Biol., 18:437-442, 2011 Cited by PubMed Abstract: We describe a phage display methodology for engineering synthetic antigen binders (sABs) that recognize either the apo or the ligand-bound conformation of maltose-binding protein (MBP). sABs that preferentially recognize the maltose-bound form of MBP act as positive allosteric effectors by substantially increasing the affinity for maltose. A crystal structure of a sAB bound to the closed form of MBP reveals the basis for this allosteric effect. We show that sABs that recognize the bound form of MBP can rescue the function of a binding-deficient mutant by restoring its natural affinity for maltose. Furthermore, the sABs can enhance maltose binding in vivo, as they provide a growth advantage to bacteria under low-maltose conditions. The results demonstrate that structure-specific sABs can be engineered to dynamically control ligand-binding affinities by modulating the transition between different conformations. PubMed: 21378967DOI: 10.1038/nsmb.2002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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