Structure of an RNA polymerase ribozyme replication complex
Strutzenberg, T. S.; Horning, D. P.; Cochrane, W. G.; Andrade, L.; Han, X.; Joyce, G. F.; Lyumkis, D.
Show abstract
Life began with the emergence of a molecule that could replicate its own genetic material, a task plausibly mediated by an RNA-dependent RNA polymerase ribozyme. Here, we present the structure of such a polymerase ribozyme, bound to RNA substrates comprising the template, primer, and nucleoside triphosphate (NTP) analog. The structure reveals how directed evolution shaped flanking elements around a highly conserved catalytic core derived from the ancestral class I ligase ribozyme. Each element serves as a functional module, positioning the primer-template duplex and incoming NTP within the active site of the enzyme. This emergent domain organization is remarkably similar to the "right hand" configuration of polymerase proteins, suggesting a common functional form for copying nucleic acids, regardless of biopolymer catalyst.
Matching journals
The top 2 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Structures of folding intermediates on BAM show diverse substrates fold by a uniform mechanism 96%
- GTP Hydrolysis by eIF5B in the Last Step of Translation Initiation Is Activated by a Rotation of the Small Ribosomal Subunit. 96%
- Structural basis for host recognition and superinfection exclusion by bacteriophage T5 95%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.