5ANR

Structure of a human 4E-T - DDX6 - CNOT1 complex

Summary for 5ANR

• Entry DOI: 10.2210/pdb5anr/pdb
• Descriptor: CCR4-NOT TRANSCRIPTION COMPLEX SUBUNIT 1, PROBABLE ATP-DEPENDENT RNA HELICASE DDX6, EUKARYOTIC TRANSLATION INITIATION FACTOR 4E TRANSPORTER, ... (4 entities in total)
• Functional Keywords: rna binding protein
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm, P-body : A5YKK6 P26196; Cytoplasm : Q9NRA8
• Total number of polymer chains: 3
• Total formula weight: 77976.94

Authors

Basquin, J.,Oezguer, S.,Conti, E. (deposition date: 2015-09-08, release date: 2015-10-21, Last modification date: 2024-01-10)

Primary citation

Ozgur, S.,Basquin, J.,Kamenska, A.,Filipowicz, W.,Standart, N.,Conti, E.
Structure of a Human 4E-T/Ddx6/Cnot1 Complex Reveals the Different Interplay of Ddx6-Binding Proteins with the Ccr4-not Complex.
Cell Rep., 13:703-, 2015

PubMed Abstract: The DEAD-box protein DDX6 is a central component of translational repression mechanisms in maternal mRNA storage in oocytes and microRNA-mediated silencing in somatic cells. DDX6 interacts with the CCR4-NOT complex and functions in concert with several post-transcriptional regulators, including Edc3, Pat1, and 4E-T. We show that the conserved CUP-homology domain (CHD) of human 4E-T interacts directly with DDX6 in both the presence and absence of the central MIF4G domain of CNOT1. The 2.1-Å resolution structure of the corresponding ternary complex reveals how 4E-T CHD wraps around the RecA2 domain of DDX6 and contacts CNOT1. Although 4E-T CHD lacks recognizable sequence similarity with Edc3 or Pat1, it shares the same DDX6-binding surface. In contrast to 4E-T, however, the Edc3 and Pat1 FDF motifs dissociate from DDX6 upon CNOT1 MIF4G binding in vitro. The results underscore the presence of a complex network of simultaneous and/or mutually exclusive interactions in DDX6-mediated repression.

PubMed: 26489469
DOI: 10.1016/J.CELREP.2015.09.033

Experimental method

X-RAY DIFFRACTION (2.102 Å)