PDBsum entry 2mkh

Translation regulator

PDB id: 2mkh

Contents

Protein chain

212 a.a.

PDB id:

2mkh

Name:

Translation regulator

Title:

Solution structure of tandem rrm domains of cytoplasmic polyadenylation element binding protein 1 (cpeb1) in free state

Structure:

Cytoplasmic polyadenylation element-binding protein 1. Chain: a. Fragment: unp residues 219-434. Synonym: cpe-bp1, cpe-binding protein 1, h-cebp, hcpeb-1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: cpeb1, cpeb. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

T.Afroz,L.Skrisovska,E.Belloc,J.G.Boixet,R.Mendez,F.H.-T.Allain

Key ref:

T.Afroz et al. (2014). A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins. Genes Dev, 28, 1498-1514. PubMed id: 24990967 DOI: 10.1101/gad.241133.114

Date:

07-Feb-14 Release date: 23-Jul-14

Protein chain

Q9BZB8  (CPEB1_HUMAN) -  Cytoplasmic polyadenylation element-binding protein 1 from Homo sapiens

Seq: 566 a.a.

Struc: 212 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1101/gad.241133.114

Genes Dev 28:1498-1514 (2014)

PubMed id: 24990967

A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins.

T.Afroz, L.Skrisovska, E.Belloc, J.Guillén-Boixet, R.Méndez, F.H.Allain.

ABSTRACT

Cytoplasmic changes in polyA tail length is a key mechanism of translational control and is implicated in germline development, synaptic plasticity, cellular proliferation, senescence, and cancer progression. The presence of a U-rich cytoplasmic polyadenylation element (CPE) in the 3' untranslated regions (UTRs) of the responding mRNAs gives them the selectivity to be regulated by the CPE-binding (CPEB) family of proteins, which recognizes RNA via the tandem RNA recognition motifs (RRMs). Here we report the solution structures of the tandem RRMs of two human paralogs (CPEB1 and CPEB4) in their free and RNA-bound states. The structures reveal an unprecedented arrangement of RRMs in the free state that undergo an original closure motion upon RNA binding that ensures high fidelity. Structural and functional characterization of the ZZ domain (zinc-binding domain) of CPEB1 suggests a role in both protein-protein and protein-RNA interactions. Together with functional studies, the structures reveal how RNA binding by CPEB proteins leads to an optimal positioning of the N-terminal and ZZ domains at the 3' UTR, which favors the nucleation of the functional ribonucleoprotein complexes for translation regulation.