6WUP の概要
| エントリーDOI | 10.2210/pdb6wup/pdb |
| 分子名称 | Ancestral cyclohexadienyl dehydratase, AncCDT-5, CHLORIDE ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total) |
| 機能のキーワード | cyclohexadienyl dehydratase ancestral protein reconstruction, lyase |
| 由来する生物種 | synthetic construct |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 27240.27 |
| 構造登録者 | |
| 主引用文献 | Kaczmarski, J.A.,Mahawaththa, M.C.,Feintuch, A.,Clifton, B.E.,Adams, L.A.,Goldfarb, D.,Otting, G.,Jackson, C.J. Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme. Nat Commun, 11:5945-5945, 2020 Cited by PubMed Abstract: Several enzymes are known to have evolved from non-catalytic proteins such as solute-binding proteins (SBPs). Although attention has been focused on how a binding site can evolve to become catalytic, an equally important question is: how do the structural dynamics of a binding protein change as it becomes an efficient enzyme? Here we performed a variety of experiments, including propargyl-DO3A-Gd(III) tagging and double electron-electron resonance (DEER) to study the rigid body protein dynamics of reconstructed evolutionary intermediates to determine how the conformational sampling of a protein changes along an evolutionary trajectory linking an arginine SBP to a cyclohexadienyl dehydratase (CDT). We observed that primitive dehydratases predominantly populate catalytically unproductive conformations that are vestiges of their ancestral SBP function. Non-productive conformational states, including a wide-open state, are frozen out of the conformational landscape via remote mutations, eventually leading to extant CDT that exclusively samples catalytically relevant compact states. These results show that remote mutations can reshape the global conformational landscape of an enzyme as a mechanism for increasing catalytic activity. PubMed: 33230119DOI: 10.1038/s41467-020-19695-9 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.49 Å) |
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