5OWF
Structure of a LAO-binding protein mutant with glutamine
Summary for 5OWF
| Entry DOI | 10.2210/pdb5owf/pdb |
| Descriptor | Lysine/arginine/ornithine-binding periplasmic protein, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (6 entities in total) |
| Functional Keywords | ligand specificity, protein design, binding pocket, periplasmatic binding protein, transport protein |
| Biological source | Salmonella typhimurium |
| Cellular location | Periplasm : P02911 |
| Total number of polymer chains | 1 |
| Total formula weight | 29930.57 |
| Authors | Shanmugaratnam, S.,Banda-Vazquez, J.,Sosa-Peinado, A.,Hocker, B. (deposition date: 2017-08-31, release date: 2018-03-21, Last modification date: 2024-11-06) |
| Primary citation | Banda-Vazquez, J.,Shanmugaratnam, S.,Rodriguez-Sotres, R.,Torres-Larios, A.,Hocker, B.,Sosa-Peinado, A. Redesign of LAOBP to bind novel l-amino acid ligands. Protein Sci., 27:957-968, 2018 Cited by PubMed Abstract: Computational protein design is still a challenge for advancing structure-function relationships. While recent advances in this field are promising, more information for genuine predictions is needed. Here, we discuss different approaches applied to install novel glutamine (Gln) binding into the Lysine/Arginine/Ornithine binding protein (LAOBP) from Salmonella typhimurium. We studied the ligand binding behavior of two mutants: a binding pocket grafting design based on a structural superposition of LAOBP to the Gln binding protein QBP from Escherichia coli and a design based on statistical coupled positions. The latter showed the ability to bind Gln even though the protein was not very stable. Comparison of both approaches highlighted a nonconservative shared point mutation between LAOBP_graft and LAOBP_sca. This context dependent L117K mutation in LAOBP turned out to be sufficient for introducing Gln binding, as confirmed by different experimental techniques. Moreover, the crystal structure of LAOBP_L117K in complex with its ligand is reported. PubMed: 29524280DOI: 10.1002/pro.3403 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.91 Å) |
Structure validation
Download full validation report
