6eoj | pdb_00006eoj

PolyA polymerase module of the cleavage and polyadenylation factor (CPF) from Saccharomyces cerevisiae

spinqualitylabelsall models 6eoj, resolution 3.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6eoj is a 3 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN NonStd Res: UNK Gene: CFT1, YHH1, YDR301W (Baker's yeast), YTH1, YPR107C (Baker's yeast), PFS2, YNL317W, N0348 (Baker's yeast) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CFT1_YEAST] RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Involved in poly(A) site recognition. May be involved in coupling transcription termination and mRNA 3'-end formation. [PFS2_YEAST] Integral and essential component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. May bridge the CPF and CFIA complexes. [YTH1_YEAST] RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Publication Abstract from PubMed Newly transcribed eukaryotic pre-mRNAs are processed at their 3'-ends by the ~1 MDa multiprotein cleavage and polyadenylation factor (CPF). CPF cleaves pre-mRNAs, adds a poly(A) tail and triggers transcription termination but it is unclear how its different enzymes are coordinated and assembled. Here, we show that the nuclease, polymerase and phosphatase activities of yeast CPF are organized into three modules. Using cryo-EM, we determine a 3.5 A resolution structure of the ~200 kDa polymerase module. This reveals four beta propellers in an assembly strikingly similar to other protein complexes that bind nucleic acid. Combined with in vitro reconstitution experiments, our data show that the polymerase module brings together factors required for specific and efficient polyadenylation, to help coordinate mRNA 3'-end processing. Architecture of eukaryotic mRNA 3'-end processing machinery.,Casanal A, Kumar A, Hill CH, Easter AD, Emsley P, Degliesposti G, Gordiyenko Y, Santhanam B, Wolf J, Wiederhold K, Dornan GL, Skehel M, Robinson CV, Passmore LA Science. 2017 Oct 26. pii: eaao6535. doi: 10.1126/science.aao6535. PMID:29074584 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA