4Q8G
Structure of the Saccharomyces cerevisiae PAN2 pseudoubiquitin-hydrolase
Summary for 4Q8G
| Entry DOI | 10.2210/pdb4q8g/pdb |
| Related | 4Q8H 4Q8J |
| Descriptor | PAB-dependent poly(A)-specific ribonuclease subunit PAN2, ZINC ION (3 entities in total) |
| Functional Keywords | ubiquitin carboxyl-terminal hydrolase-like domain, uch, pan3, inactive, hydrolase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Cytoplasm: P53010 |
| Total number of polymer chains | 2 |
| Total formula weight | 106728.94 |
| Authors | Schaefer, I.B.,Conti, E. (deposition date: 2014-04-27, release date: 2014-06-04, Last modification date: 2024-02-28) |
| 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 (2.1 Å) |
Structure validation
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