Summary for 4XR7
| Entry DOI | 10.2210/pdb4xr7/pdb |
| Related | 4Q8G 4Q8H |
| Descriptor | PAB-dependent poly(A)-specific ribonuclease subunit PAN2, PAB-dependent poly(A)-specific ribonuclease subunit PAN3 (2 entities in total) |
| Functional Keywords | rna degradation, deadenylation, hydrolase, pseudokinase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Cellular location | Cytoplasm : P53010 P36102 |
| Total number of polymer chains | 12 |
| Total formula weight | 791698.28 |
| Authors | Schafer, I.B.,Rode, M.,Bonneau, F.,Schussler, S.,Conti, E. (deposition date: 2015-01-20, release date: 2015-01-28, Last modification date: 2024-05-08) |
| Primary citation | Schafer, I.B.,Rode, M.,Bonneau, F.,Schussler, S.,Conti, E. The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase. Nat. Struct. Mol. Biol., 21:591-598, 2014 Cited by PubMed Abstract: Pan2-Pan3 is a conserved complex involved in the shortening of mRNA poly(A) tails, the initial step in eukaryotic mRNA turnover. We show that recombinant Saccharomyces cerevisiae Pan2-Pan3 can deadenylate RNAs in vitro without needing the poly(A)-binding protein Pab1. The crystal structure of an active ~200-kDa core complex reveals that Pan2 and Pan3 interact with an unusual 1:2 stoichiometry imparted by the asymmetric nature of the Pan3 homodimer. An extended region of Pan2 wraps around Pan3 and provides a major anchoring point for complex assembly. A Pan2 module formed by the pseudoubiquitin-hydrolase and RNase domains latches onto the Pan3 pseudokinase with intertwined interactions that orient the deadenylase active site toward the A-binding site of the interacting Pan3. The molecular architecture of Pan2-Pan3 suggests how the nuclease and its pseudokinase regulator act in synergy to promote deadenylation. PubMed: 24880344DOI: 10.1038/nsmb.2834 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.796 Å) |
Structure validation
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