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PDBsum entry 4xr7
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683 a.a.
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441 a.a.
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414 a.a.
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PDB id:
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Hydrolase
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Title:
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Structure of the saccharomyces cerevisiae pan2-pan3 core complex
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Structure:
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Pab-dependent poly(a)-specific ribonuclease subunit pan2. Chain: g, d, j, a. Synonym: pab1p-dependent poly(a)-nuclease,pan deadenylation complex catalytic subunit 2. Engineered: yes. Pab-dependent poly(a)-specific ribonuclease subunit pan3. Chain: l, k, e, f, h, i, c, b. Synonym: pab1p-dependent poly(a)-nuclease,pan deadenylation complex subunit 3.
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: pan2, ygl094c. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Gene: pan3, ecm35, ykl025c. Expression_system_taxid: 7111
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Resolution:
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3.80Å
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R-factor:
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0.286
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R-free:
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0.299
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Authors:
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I.B.Schafer,M.Rode,F.Bonneau,S.Schussler,E.Conti
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Key ref:
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I.B.Schäfer
et al.
(2014).
The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase.
Nat Struct Biol,
21,
591-598.
PubMed id:
DOI:
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Date:
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20-Jan-15
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Release date:
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28-Jan-15
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Supersedes:
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PROCHECK
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Headers
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References
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P53010
(PAN2_YEAST) -
PAN2-PAN3 deadenylation complex catalytic subunit PAN2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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1115 a.a.
683 a.a.
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Enzyme class 2:
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Chains G, D, J, A:
E.C.3.1.13.4
- poly(A)-specific ribonuclease.
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Reaction:
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Exonucleolytic cleavage of poly(A) to 5'-AMP.
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Enzyme class 3:
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Chains L, K, E, F, H, I, C, B:
E.C.?
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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DOI no:
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Nat Struct Biol
21:591-598
(2014)
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PubMed id:
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The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase.
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I.B.Schäfer,
M.Rode,
F.Bonneau,
S.Schüssler,
E.Conti.
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ABSTRACT
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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.
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Links
