Literature summary extracted from
Nakel, K.; Bonneau, F.; Eckmann, C.R.; Conti, E.
Structural basis for the activation of the C. elegans noncanonical cytoplasmic poly(A)-polymerase GLD-2 by GLD-3 (2015), Proc. Natl. Acad. Sci. USA, 112, 8614-8619.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.7.19 |
germ-line development defective GLD-2GLD-3 complex up-regulates the expression of genes required for meiotic progression. The structure of a minimal polyadenylation complex that includes the conserved nucleotidyl-transferase core of GLD-2 and the N-terminal domain of GLD-3, to 2.3 A resolution, shows that the N-terminal domain of GLD-3 does not fold into the predicted multi-K homology domain but wraps around the catalytic domain of GLD-2. GLD-3 activates GLD-2 both indirectly by stabilizing the enzyme and directly by contributing positively charged residues near the RNA-binding cleft. Due to distinct structural features, GLD-2 displays unusual specificity in vitro for single-stranded RNAs with at least one adenosine at the 3'-end |
Caenorhabditis elegans |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.7.19 |
Caenorhabditis elegans |
O17087 |
- |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.7.19 |
ATP + RNA primer |
isoform GLD-2 shows specificity in vitro for single-stranded RNAs with at least one adenosine at the 3'-end |
Caenorhabditis elegans |
diphosphate + RNA primer-A |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.7.19 |
GLD-2 |
- |
Caenorhabditis elegans |