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2XZ2

Crystal structure of CstF-50 homodimerization domain

Summary for 2XZ2
Entry DOI10.2210/pdb2xz2/pdb
DescriptorCSTF-50, ISOFORM B, SODIUM ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
Functional Keywordsrna-binding protein, 3' end mrna maturation, transcription, rna binding protein
Biological sourceDROSOPHILA MELANOGASTER (FRUIT FLY)
Total number of polymer chains1
Total formula weight7846.14
Authors
Moreno-Morcillo, M.,Fribourg, S. (deposition date: 2010-11-22, release date: 2011-01-26, Last modification date: 2024-05-08)
Primary citationMoreno-Morcillo, M.,Minvielle-Sebastia, L.,Mackereth, C.,Fribourg, S.
Hexameric Architecture of Cstf Supported by Cstf- 50 Homodimerization Domain Structure.
RNA, 17:412-, 2011
Cited by
PubMed Abstract: The Cleavage stimulation Factor (CstF) complex is composed of three subunits and is essential for pre-mRNA 3'-end processing. CstF recognizes U and G/U-rich cis-acting RNA sequence elements and helps stabilize the Cleavage and Polyadenylation Specificity Factor (CPSF) at the polyadenylation site as required for productive RNA cleavage. Here, we describe the crystal structure of the N-terminal domain of Drosophila CstF-50 subunit. It forms a compact homodimer that exposes two geometrically opposite, identical, and conserved surfaces that may serve as binding platform. Together with previous data on the structure of CstF-77, homodimerization of CstF-50 N-terminal domain supports the model in which the functional state of CstF is a heterohexamer.
PubMed: 21233223
DOI: 10.1261/RNA.2481011
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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数据于2025-06-25公开中

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