PDBsum entry 4xr7

Hydrolase

PDB id: 4xr7

Contents

Protein chains

683 a.a.

441 a.a.

414 a.a.

PDB id:

4xr7

Name:

Hydrolase

Title:

Structure of the saccharomyces cerevisiae pan2-pan3 core complex

Structure:

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.

Source:

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

Resolution:

3.80Å R-factor: 0.286 R-free: 0.299

Authors:

I.B.Schafer,M.Rode,F.Bonneau,S.Schussler,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:

20-Jan-15 Release date: 28-Jan-15

Supersedes:

4q8j

Protein chains

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

Seq: 1115 a.a.

Struc: 683 a.a.

Protein chains

P36102  (PAN3_YEAST) -  PAN2-PAN3 deadenylation complex subunit PAN3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 679 a.a.

Struc: 441 a.a.

Protein chains

P36102  (PAN3_YEAST) -  PAN2-PAN3 deadenylation complex subunit PAN3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 679 a.a.

Struc: 414 a.a.

Enzyme reactions

• Enzyme class 2: Chains G, D, J, A: E.C.3.1.13.4 - poly(A)-specific ribonuclease.
• Reaction: Exonucleolytic cleavage of poly(A) to 5'-AMP.
• Enzyme class 3: Chains L, K, E, F, H, I, C, B: E.C.?

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.

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.