6F9S

Crystal structure of the C-terminal RecA domain of DDX6 in complex with a conserved peptide from LSM14

Summary for 6F9S

• Entry DOI: 10.2210/pdb6f9s/pdb
• Descriptor: Probable ATP-dependent RNA helicase DDX6, Cytokinesis, Apoptosis, RNA-associated, SULFATE ION, ... (4 entities in total)
• Functional Keywords: mrna turnover, translational repression, decapping, rna
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm, P-body : P26196
• Total number of polymer chains: 2
• Total formula weight: 30629.53

Authors

Jinek, M.,Brandmann, T. (deposition date: 2017-12-15, release date: 2018-03-21, Last modification date: 2024-01-17)

Primary citation

Brandmann, T.,Fakim, H.,Padamsi, Z.,Youn, J.Y.,Gingras, A.C.,Fabian, M.R.,Jinek, M.
Molecular architecture of LSM14 interactions involved in the assembly of mRNA silencing complexes.
EMBO J., 37:-, 2018

PubMed Abstract: The LSM domain-containing protein LSM14/Rap55 plays a role in mRNA decapping, translational repression, and RNA granule (P-body) assembly. How LSM14 interacts with the mRNA silencing machinery, including the eIF4E-binding protein 4E-T and the DEAD-box helicase DDX6, is poorly understood. Here we report the crystal structure of the LSM domain of LSM14 bound to a highly conserved C-terminal fragment of 4E-T. The 4E-T C-terminus forms a bi-partite motif that wraps around the N-terminal LSM domain of LSM14. We also determined the crystal structure of LSM14 bound to the C-terminal RecA-like domain of DDX6. LSM14 binds DDX6 via a unique non-contiguous motif with distinct directionality as compared to other DDX6-interacting proteins. Together with mutational and proteomic studies, the LSM14-DDX6 structure reveals that LSM14 has adopted a divergent mode of binding DDX6 in order to support the formation of mRNA silencing complexes and P-body assembly.

PubMed: 29510985
DOI: 10.15252/embj.201797869

Experimental method

X-RAY DIFFRACTION (3.03 Å)