In-line alignment and Mg2+ coordination at the cleavage site of the env22 twister ribozyme Journal Article


Authors: Ren, A.; Kosutic, M.; Rajashankar, K. R.; Frener, M.; Santner, T.; Westhof, E.; Micura, R.; Patel, D. J.
Article Title: In-line alignment and Mg2+ coordination at the cleavage site of the env22 twister ribozyme
Abstract: Small self-cleaving nucleolytic ribozymes contain catalytic domains that accelerate site-specific cleavage/ligation of phosphodiester backbones. We report on the 2.9-angstrom crystal structure of the env22 twister ribozyme, which adopts a compact tertiary fold stabilized by co-helical stacking, double-pseudoknot formation and long-range pairing interactions. The U-A cleavage site adopts a splayed-apart conformation with the modelled 2'-O of U positioned for in-line attack on the adjacent to-be-cleaved P-O5' bond. Both an invariant guanosine and a Mg2+ are directly coordinated to the non-bridging phosphate oxygens at the U-A cleavage step, with the former positioned to contribute to catalysis and the latter to structural integrity. The impact of key mutations on cleavage activity identified an invariant guanosine that contributes to catalysis. Our structure of the in-line aligned env22 twister ribozyme is compared with two recently reported twister ribozymes structures, which adopt similar global folds, but differ in conformational features around the cleavage site.
Keywords: catalysis; crystal-structure; structural basis; mechanisms; hepatitis-delta-virus; group-ii intron; self-cleaving ribozymes; hairpin ribozyme; satellite rna; splicing rna
Journal Title: Nature Communications
Volume: 5
ISSN: 2041-1723
Publisher: Nature Publishing Group  
Date Published: 2014-11-20
Start Page: 5534
Language: English
ACCESSION: WOS:000345622500011
DOI: 10.1038/ncomms6534
PROVIDER: wos
PUBMED: 25410397
PMCID: PMC4373348
Notes: Article -- 5534 -- 10 page article-- Source: Wos
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  1. Dinshaw J Patel
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  2. Aiming Ren
    11 Ren