4EMG

Crystal structure of SpLsm3

Summary for 4EMG

• Entry DOI: 10.2210/pdb4emg/pdb
• Descriptor: Probable U6 snRNA-associated Sm-like protein LSm3 (2 entities in total)
• Functional Keywords: sm fold, mrna decay, lsm proteins, rna binding protein
• Biological source: Schizosaccharomyces pombe (Fission yeast)
• Cellular location: Nucleus (By similarity): Q9Y7M4
• Total number of polymer chains: 14
• Total formula weight: 151491.66

Authors

Jiang, S.M.,Wu, D.H.,Song, H.W. (deposition date: 2012-04-12, release date: 2012-06-13, Last modification date: 2024-10-30)

Primary citation

Wu, D.H.,Jiang, S.M.,Bowler, M.W.,Song, H.W.
Crystal Structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces pombe.
Plos One, 7:e36768-e36768, 2012

PubMed Abstract: Sm-like (Lsm) proteins are ubiquitous and function in many aspects of RNA metabolism, including pre-mRNA splicing, nuclear RNA processing, mRNA decay and miRNA biogenesis. Here three crystal structures including Lsm3, Lsm4 and Lsm5/6/7 sub-complex from S. pombe are reported. These structures show that all the five individual Lsm subunits share a conserved Sm fold, and Lsm3, Lsm4, and Lsm5/6/7 form a heptamer, a trimer and a hexamer within the crystal lattice, respectively. Analytical ultracentrifugation indicates that Lsm3 and Lsm5/6/7 sub-complex exist in solution as a heptamer and a hexamer, respectively while Lsm4 undergoes a dynamic equilibrium between monomer and trimer in solution. RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.

PubMed: 22615807
DOI: 10.1371/journal.pone.0036768

Experimental method

X-RAY DIFFRACTION (2.7 Å)