PDBsum entry 4czy

Gene regulation

PDB id: 4czy

Contents

Protein chains

323 a.a.

403 a.a.

Ligands

MES ×2

ANP ×2

Metals

_MG ×2

PDB id:

4czy

Name:

Gene regulation

Title:

Complex of neurospora crassa pan2 (wd40-cs1) with pan3 (pseudokinase and c-term)

Structure:

Pab-dependent poly(a)-specific ribonuclease subunit pan2. Chain: a, c. Fragment: wd40 domain and cs1 region, residues 1-351. Synonym: pab1p-dependent poly(a)-nuclease, pan deadenylation complex catalytic subunit 2, a-specific ribonuclease subunit pan2. Engineered: yes. Pab-dependent poly(a)-specific ribonuclease subunit pan3. Chain: b, d. Fragment: pseudokinase domain and c-term, residues 234-656.

Source:

Neurospora crassa. Organism_taxid: 5141. Atcc: 24698. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: star.

Resolution:

3.40Å R-factor: 0.223 R-free: 0.263

Authors:

S.Jonas,E.Izaurralde,O.Weichenrieder

Key ref:

S.Jonas et al. (2014). An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decay. Nat Struct Biol, 21, 599-608. PubMed id: 24880343 DOI: 10.1038/nsmb.2837

Date:

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

Protein chains

P0C581  (PAN2_NEUCR) -  PAN2-PAN3 deadenylation complex catalytic subunit pan2 from Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

Seq: 1310 a.a.

Struc: 323 a.a.

Protein chains

Q7SDP4  (PAN3_NEUCR) -  PAN2-PAN3 deadenylation complex subunit pan3 from Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

Seq: 656 a.a.

Struc: 403 a.a.

Enzyme reactions

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

DOI no: 10.1038/nsmb.2837

Nat Struct Biol 21:599-608 (2014)

PubMed id: 24880343

An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decay.

S.Jonas, M.Christie, D.Peter, D.Bhandari, B.Loh, E.Huntzinger, O.Weichenrieder, E.Izaurralde.

ABSTRACT

The PAN2-PAN3 complex functions in general and microRNA-mediated mRNA deadenylation. However, mechanistic insight into PAN2 and its complex with the asymmetric PAN3 dimer is lacking. Here, we describe crystal structures that show that Neurospora crassa PAN2 comprises two independent structural units: a C-terminal catalytic unit and an N-terminal assembly unit that engages in a bipartite interaction with PAN3 dimers. The catalytic unit contains the exonuclease domain in an intimate complex with a potentially modulatory ubiquitin-protease-like domain. The assembly unit contains a WD40 propeller connected to an adaptable linker. The propeller contacts the PAN3 C-terminal domain, whereas the linker reinforces the asymmetry of the PAN3 dimer and prevents the recruitment of a second PAN2 molecule. Functional data indicate an essential role for PAN3 in coordinating PAN2-mediated deadenylation with subsequent steps in mRNA decay, which lead to complete mRNA degradation.