4N0A

Crystal structure of Lsm2-3-Pat1C complex from Saccharomyces cerevisiae

Summary for 4N0A

• Entry DOI: 10.2210/pdb4n0a/pdb
• Descriptor: U6 snRNA-associated Sm-like protein LSm3, U6 snRNA-associated Sm-like protein LSm2, DNA topoisomerase 2-associated protein PAT1, ... (4 entities in total)
• Functional Keywords: decapping activator, rna binding protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus: P57743 P38203; Cytoplasm: P25644
• Total number of polymer chains: 10
• Total formula weight: 208118.21

Authors

Wu, D.H. (deposition date: 2013-10-01, release date: 2013-12-04, Last modification date: 2024-03-20)

Primary citation

Wu, D.,Muhlrad, D.,Bowler, M.W.,Jiang, S.,Liu, Z.,Parker, R.,Song, H.
Lsm2 and Lsm3 bridge the interaction of the Lsm1-7 complex with Pat1 for decapping activation
Cell Res., 24:233-246, 2014

PubMed Abstract: The evolutionarily conserved Lsm1-7-Pat1 complex is the most critical activator of mRNA decapping in eukaryotic cells and plays many roles in normal decay, AU-rich element-mediated decay, and miRNA silencing, yet how Pat1 interacts with the Lsm1-7 complex is unknown. Here, we show that Lsm2 and Lsm3 bridge the interaction between the C-terminus of Pat1 (Pat1C) and the Lsm1-7 complex. The Lsm2-3-Pat1C complex and the Lsm1-7-Pat1C complex stimulate decapping in vitro to a similar extent and exhibit similar RNA-binding preference. The crystal structure of the Lsm2-3-Pat1C complex shows that Pat1C binds to Lsm2-3 to form an asymmetric complex with three Pat1C molecules surrounding a heptameric ring formed by Lsm2-3. Structure-based mutagenesis revealed the importance of Lsm2-3-Pat1C interactions in decapping activation in vivo. Based on the structure of Lsm2-3-Pat1C, a model of Lsm1-7-Pat1 complex is constructed and how RNA binds to this complex is discussed.

PubMed: 24247251
DOI: 10.1038/cr.2013.152

Experimental method

X-RAY DIFFRACTION (3.15 Å)