6AHW

Crystal structure of circular-permutated YibK methyltransferase from Haemophilus influenzae

6AHW の概要

• エントリーDOI: 10.2210/pdb6ahw/pdb
• 分子名称: circular-permutated tRNA (cytidine(34)-2'-O)-methyltransferase (2 entities in total)
• 機能のキーワード: transferase, methyltransferase, circular permutation
• 由来する生物種: Haemophilus influenzae Rd KW20; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37405.48

構造登録者

Chuang, Y.C.,Lyu, P.C.,Hsu, S.T.D. (登録日: 2018-08-20, 公開日: 2019-01-23, 最終更新日: 2024-03-27)

主引用文献

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

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: 30639189
DOI: 10.1016/j.jmb.2019.01.005

実験手法

X-RAY DIFFRACTION (1.56 Å)