3TP2

Crystal Structure of the Splicing Factor Cwc2 from yeast

Summary for 3TP2

• Entry DOI: 10.2210/pdb3tp2/pdb
• Descriptor: Pre-mRNA-splicing factor CWC2, SODIUM ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: rna scaffold, torus domain, ccch zinc finger, rrm domain, splicing
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Nucleus: Q12046
• Total number of polymer chains: 2
• Total formula weight: 52218.09

Authors

Schmitzova, J. (deposition date: 2011-09-07, release date: 2012-03-14, Last modification date: 2024-02-28)

Primary citation

Schmitzova, J.,Rasche, N.,Dybkov, O.,Kramer, K.,Fabrizio, P.,Urlaub, H.,Luhrmann, R.,Pena, V.
Crystal structure of Cwc2 reveals a novel architecture of a multipartite RNA-binding protein.
Embo J., 31:2222-2234, 2012

PubMed Abstract: The yeast splicing factor Cwc2 contacts several catalytically important RNA elements in the active spliceosome, suggesting that Cwc2 is involved in determining their spatial arrangement at the spliceosome's catalytic centre. We have determined the crystal structure of the Cwc2 functional core, revealing how a previously uncharacterized Torus domain, an RNA recognition motif (RRM) and a zinc finger (ZnF) are tightly integrated in a compact folding unit. The ZnF plays a pivotal role in the architecture of the whole assembly. UV-induced crosslinking of Cwc2-U6 snRNA allowed the identification by mass spectrometry of six RNA-contacting sites: four in or close to the RRM domain, one in the ZnF and one on a protruding element connecting the Torus and RRM domains. The three distinct regions contacting RNA are connected by a contiguous and conserved positively charged surface, suggesting an expanded interface for RNA accommodation. Cwc2 mutations confirmed that the connector element plays a crucial role in splicing. We conclude that Cwc2 acts as a multipartite RNA-binding platform to bring RNA elements of the spliceosome's catalytic centre into an active conformation.

PubMed: 22407296
DOI: 10.1038/emboj.2012.58

Experimental method

X-RAY DIFFRACTION (2.4 Å)