6AHW
Crystal structure of circular-permutated YibK methyltransferase from Haemophilus influenzae
Summary for 6AHW
| Entry DOI | 10.2210/pdb6ahw/pdb |
| Descriptor | circular-permutated tRNA (cytidine(34)-2'-O)-methyltransferase (2 entities in total) |
| Functional Keywords | transferase, methyltransferase, circular permutation |
| Biological source | Haemophilus influenzae Rd KW20 More |
| Total number of polymer chains | 2 |
| Total formula weight | 37405.48 |
| Authors | Chuang, Y.C.,Lyu, P.C.,Hsu, S.T.D. (deposition date: 2018-08-20, release date: 2019-01-23, Last modification date: 2024-03-27) |
| Primary citation | Chuang, Y.C.,Hu, I.C.,Lyu, P.C.,Hsu, S.D. Untying a Protein Knot by Circular Permutation. J. Mol. Biol., 431:857-863, 2019 Cited by PubMed Abstract: Topologically knotted proteins are tantalizing examples of how polypeptide chains can explore complex free energy landscapes to efficiently attain defined knotted conformations. The evolution trails of protein knots, however, remain elusive. We used circular permutation to change an evolutionally conserved topologically knotted SPOUT RNA methyltransferase into an unknotted form. The unknotted variant adopted the same three-dimensional structure and oligomeric state as its knotted parent, but its folding stability was markedly reduced with accelerated folding kinetics and its ligand binding was abrogated. Our findings support the hypothesis that the universally conserved knotted topology of the SPOUT superfamily evolved from unknotted forms through circular permutation under selection pressure for folding robustness and, more importantly, for functional requirements associated with the knotted structural element. PubMed: 30639189DOI: 10.1016/j.jmb.2019.01.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
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