7QSQ
Permutated N-terminal lobe of the ribose binding protein from Thermotoga maritima
Summary for 7QSQ
| Entry DOI | 10.2210/pdb7qsq/pdb |
| Descriptor | Ribose ABC transporter, periplasmic ribose-binding protein, SULFATE ION, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | solute binding protein, circular permutation, periplasmic binding proteins, domain swapping, sugar binding protein |
| Biological source | Thermotoga maritima More |
| Total number of polymer chains | 4 |
| Total formula weight | 61879.61 |
| Authors | Shanmugaratnam, S.,Michel, F.,Hocker, B. (deposition date: 2022-01-14, release date: 2023-01-11, Last modification date: 2024-01-31) |
| Primary citation | Michel, F.,Shanmugaratnam, S.,Romero-Romero, S.,Hocker, B. Structures of permuted halves of a modern ribose-binding protein. Acta Crystallogr D Struct Biol, 79:40-49, 2023 Cited by PubMed Abstract: Periplasmic binding proteins (PBPs) are a class of proteins that participate in the cellular transport of various ligands. They have been used as model systems to study mechanisms in protein evolution, such as duplication, recombination and domain swapping. It has been suggested that PBPs evolved from precursors half their size. Here, the crystal structures of two permuted halves of a modern ribose-binding protein (RBP) from Thermotoga maritima are reported. The overexpressed proteins are well folded and show a monomer-dimer equilibrium in solution. Their crystal structures show partially noncanonical PBP-like fold type I conformations with structural deviations from modern RBPs. One of the half variants forms a dimer via segment swapping, suggesting a high degree of malleability. The structural findings on these permuted halves support the evolutionary hypothesis that PBPs arose via a duplication event of a flavodoxin-like protein and further support a domain-swapping step that might have occurred during the evolution of the PBP-like fold, a process that is necessary to generate the characteristic motion of PBPs essential to perform their functions. PubMed: 36601806DOI: 10.1107/S205979832201186X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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