2UY1

CRYSTAL STRUCTURE OF CSTF-77

Summary for 2UY1

• Entry DOI: 10.2210/pdb2uy1/pdb
• Descriptor: CLEAVAGE STIMULATION FACTOR 77 (3 entities in total)
• Functional Keywords: rna-binding protein, rna binding protein
• Biological source: ENCEPHALITOZOON CUNICULI; More
• Total number of polymer chains: 2
• Total formula weight: 116450.78

Authors

Legrand, P.,Pinaud, N.,Minvielle-Sebastia, L.,Fribourg, S. (deposition date: 2007-04-02, release date: 2007-07-03, Last modification date: 2024-05-08)

Primary citation

Legrand, P.,Pinaud, N.,Minvielle-Sebastia, L.,Fribourg, S.
The Structure of the Cstf-77 Homodimer Provides Insights Into Cstf Assembly.
Nucleic Acids Res., 35:4515-, 2007

PubMed Abstract: The cleavage stimulation factor (CstF) is essential for the first step of poly(A) tail formation at the 3' ends of mRNAs. This heterotrimeric complex is built around the 77-kDa protein bridging both CstF-64 and CstF-50 subunits. We have solved the crystal structure of the 77-kDa protein from Encephalitozoon cuniculi at a resolution of 2 A. The structure folds around 11 Half-a-TPR repeats defining two domains. The crystal structure reveals a tight homodimer exposing phylogenetically conserved areas for interaction with protein partners. Mapping experiments identify the C-terminal region of Rna14p, the yeast counterpart of CstF-77, as the docking domain for Rna15p, the yeast CstF-64 homologue.

PubMed: 17584787
DOI: 10.1093/NAR/GKM458

Experimental method

X-RAY DIFFRACTION (2 Å)