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8B7T

CPSF73 CTD3

Summary for 8B7T
Entry DOI10.2210/pdb8b7t/pdb
NMR InformationBMRB: 34760
DescriptorCPSF73 (1 entity in total)
Functional Keywordscleavage and polyadenylation specifity factor, rna binding protein
Biological sourceEncephalitozoon cuniculi
Total number of polymer chains1
Total formula weight8498.00
Authors
Thore, S.,Mackereth, C. (deposition date: 2022-10-03, release date: 2023-05-03, Last modification date: 2023-12-06)
Primary citationThore, S.,Raoelijaona, F.,Talenton, V.,Fribourg, S.,Mackereth, C.D.
Molecular details of the CPSF73-CPSF100 C-terminal heterodimer and interaction with Symplekin.
Open Biology, 13:230221-230221, 2023
Cited by
PubMed Abstract: Eukaryotic pre-mRNA is processed by a large multiprotein complex to accurately cleave the 3' end, and to catalyse the addition of the poly(A) tail. Within this cleavage and polyadenylation specificity factor (CPSF) machinery, the CPSF73/CPSF3 endonuclease subunit directly contacts both CPSF100/CPSF2 and the scaffold protein Symplekin to form a subcomplex known as the core cleavage complex or mammalian cleavage factor. Here we have taken advantage of a stable CPSF73-CPSF100 minimal heterodimer from to determine the solution structure formed by the first and second C-terminal domain (CTD1 and CTD2) of both proteins. We find a large number of contacts between both proteins in the complex, and notably in the region between CTD1 and CTD2. A similarity is also observed between CTD2 and the TATA-box binding protein (TBP) domains. Separately, we have determined the structure of the terminal CTD3 domain of CPSF73, which also belongs to the TBP domain family and is connected by a flexible linker to the rest of CPSF73. Biochemical assays demonstrate a key role for the CTD3 of CPSF73 in binding Symplekin, and structural models of the trimeric complex from other species allow for comparative analysis and support an overall conserved architecture.
PubMed: 37989222
DOI: 10.1098/rsob.230221
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227344

数据于2024-11-13公开中

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