4C92

Crystal structure of the yeast Lsm1-7 complex

Summary for 4C92

• Entry DOI: 10.2210/pdb4c92/pdb
• Related: 4C8Q
• Descriptor: SM-LIKE PROTEIN LSM1, U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM2, U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM3, ... (8 entities in total)
• Functional Keywords: transcription, lsm1-7, decapping activators, mrna degradation
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Nucleus: P47017 P38203 P57743 P40070 P40089 P53905; Cytoplasm: Q06406
• Total number of polymer chains: 7
• Total formula weight: 85445.86

Authors

Sharif, H.,Conti, E. (deposition date: 2013-10-02, release date: 2013-10-16, Last modification date: 2023-12-20)

Primary citation

Sharif, H.,Conti, E.
Architecture of the Lsm1-7-Pat1 Complex: A Conserved Assembly in Eukaryotic Mrna Turnover
Cell Rep., 5:283-, 2013

PubMed Abstract: The decay of mRNAs is a key step in eukaryotic gene expression. The cytoplasmic Lsm1-7-Pat1 complex is a conserved component of the 5'-to-3' mRNA decay pathway, linking deadenylation to decapping. Lsm1-7 is similar to the nuclear Sm complexes that bind oligo-uridine tracts in snRNAs. The 2.3 Å resolution structure of S. cerevisiae Lsm1-7 shows the presence of a heptameric ring with Lsm1-2-3-6-5-7-4 topology. A distinct structural feature of the cytoplasmic Lsm ring is the C-terminal extension of Lsm1, which plugs the exit site of the central channel and approaches the RNA binding pockets. The 3.7 Å resolution structure of Lsm1-7 bound to the C-terminal domain of Pat1 reveals that Pat1 recognition is not mediated by the distinguishing cytoplasmic subunit, Lsm1, but by Lsm2 and Lsm3. These results show how the auxiliary domains and the canonical Sm folds of the Lsm1-7 complex are organized in order to mediate and modulate macromolecular interactions.

PubMed: 24139796
DOI: 10.1016/J.CELREP.2013.10.004

Experimental method

X-RAY DIFFRACTION (2.299 Å)