7JH1
Solution structure of a reconstructed XCL1 ancestor
Summary for 7JH1
| Entry DOI | 10.2210/pdb7jh1/pdb |
| NMR Information | BMRB: 30777 |
| Descriptor | XCL1 ancestor (1 entity in total) |
| Functional Keywords | metamorphic protein, chemokine, ancestral reconstruction, cytokine |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 7483.08 |
| Authors | Tyler, R.C.,Peterson, F.C.,Volkman, B.F. (deposition date: 2020-07-20, release date: 2020-12-30, Last modification date: 2024-10-30) |
| Primary citation | Dishman, A.F.,Tyler, R.C.,Fox, J.C.,Kleist, A.B.,Prehoda, K.E.,Babu, M.M.,Peterson, F.C.,Volkman, B.F. Evolution of fold switching in a metamorphic protein. Science, 371:86-90, 2021 Cited by PubMed Abstract: Metamorphic proteins switch between different folds, defying the protein folding paradigm. It is unclear how fold switching arises during evolution. With ancestral reconstruction and nuclear magnetic resonance, we studied the evolution of the metamorphic human protein XCL1, which has two distinct folds with different functions, making it an unusual member of the chemokine family, whose members generally adopt one conserved fold. XCL1 evolved from an ancestor with the chemokine fold. Evolution of a dimer interface, changes in structural constraints and molecular strain, and alteration of intramolecular protein contacts drove the evolution of metamorphosis. Then, XCL1 likely evolved to preferentially populate the noncanonical fold before reaching its modern-day near-equal population of folds. These discoveries illuminate how one sequence has evolved to encode multiple structures, revealing principles for protein design and engineering. PubMed: 33384377DOI: 10.1126/science.abd8700 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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