PDBsum entry 4q8h

Hydrolase

PDB id: 4q8h

Contents

Protein chain

627 a.a.

Metals

_MG ×2

PDB id:

4q8h

Name:

Hydrolase

Title:

Structure of the saccharomyces cerevisiae pan2 pseudoubiquitin- hydrolase-rnase module

Structure:

Pab-dependent poly(a)-specific ribonuclease subunit pan2. Chain: a. Fragment: unp residues 460-1115. Synonym: pab1p-dependent poly(a)-nuclease, pan deadenylation complex catalytic subunit 2. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: pan2, ygl094c. Expressed in: trichoplusia ni. Expression_system_taxid: 7111.

Resolution:

3.10Å R-factor: 0.241 R-free: 0.275

Authors:

I.B.Schaefer,E.Conti

Key ref:

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: 24880344 DOI: 10.1038/nsmb.2834

Date:

27-Apr-14 Release date: 04-Jun-14

Protein chain

P53010  (PAN2_YEAST) -  PAN2-PAN3 deadenylation complex catalytic subunit PAN2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 1115 a.a.

Struc: 627 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.1.13.4 - poly(A)-specific ribonuclease.
• Reaction: Exonucleolytic cleavage of poly(A) to 5'-AMP.

DOI no: 10.1038/nsmb.2834

Nat Struct Biol 21:591-598 (2014)

PubMed id: 24880344

The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase.

I.B.Schäfer, M.Rode, F.Bonneau, S.Schüssler, E.Conti.

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.