Structural highlights
Function
[TRML_HAEIN] Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide.[HAMAP-Rule:MF_01885]
Publication Abstract from PubMed
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.
Untying a Protein Knot by Circular Permutation.,Chuang YC, Hu IC, Lyu PC, Hsu SD J Mol Biol. 2019 Jan 9. pii: S0022-2836(19)30007-5. doi:, 10.1016/j.jmb.2019.01.005. PMID:30639189[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chuang YC, Hu IC, Lyu PC, Hsu SD. Untying a Protein Knot by Circular Permutation. J Mol Biol. 2019 Jan 9. pii: S0022-2836(19)30007-5. doi:, 10.1016/j.jmb.2019.01.005. PMID:30639189 doi:http://dx.doi.org/10.1016/j.jmb.2019.01.005
