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6URO

Cryo-EM structure of human CPSF160-WDR33-CPSF30-PAS RNA-CstF77 complex

Summary for 6URO
Entry DOI10.2210/pdb6uro/pdb
Related6URG
EMDB information20859 20860 20861
DescriptorCleavage and polyadenylation specificity factor subunit 1, pre-mRNA 3' end processing protein WDR33, Cleavage and polyadenylation specificity factor subunit 4, ... (6 entities in total)
Functional Keywordspre-mrna 3'-end processing, rna binding, aauaaa polyadenylation signal, rna binding protein-rna complex, mpsf, rna binding protein/rna
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains6
Total formula weight438138.06
Authors
Sun, Y.,Zhang, Y.,Walz, T.,Tong, L. (deposition date: 2019-10-23, release date: 2019-11-27, Last modification date: 2025-05-28)
Primary citationZhang, Y.,Sun, Y.,Shi, Y.,Walz, T.,Tong, L.
Structural Insights into the Human Pre-mRNA 3'-End Processing Machinery.
Mol.Cell, 77:800-, 2020
Cited by
PubMed Abstract: The mammalian pre-mRNA 3'-end-processing machinery consists of cleavage and polyadenylation specificity factor (CPSF), cleavage stimulation factor (CstF), and other proteins, but the overall architecture of this machinery remains unclear. CPSF contains two functionally distinct modules: a cleavage factor (mCF) and a polyadenylation specificity factor (mPSF). Here, we have produced recombinant human CPSF and CstF and examined these factors by electron microscopy (EM). We find that mPSF is the organizational core of the machinery, while the conformations of mCF and CstF and the position of mCF relative to mPSF are highly variable. We have identified by cryo-EM a segment in CPSF100 that tethers mCF to mPSF, and we have named it the PSF interaction motif (PIM). Mutations in the PIM can abolish CPSF formation, indicating that it is a crucial contact in CPSF. We have also obtained reconstructions of mCF and CstF77 by cryo-EM, assembled around the mPSF core.
PubMed: 31810758
DOI: 10.1016/j.molcel.2019.11.005
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

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건을2026-02-11부터공개중

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