2NAX
Structure of CCHC zinc finger domain of Pcf11
Summary for 2NAX
| Entry DOI | 10.2210/pdb2nax/pdb |
| NMR Information | BMRB: 25953 |
| Descriptor | Protein PCF11, ZINC ION (2 entities in total) |
| Functional Keywords | zinc finger, metal binding protein |
| Biological source | Saccharomyces cerevisiae S288c (Baker's yeast) |
| Cellular location | Nucleus : P39081 |
| Total number of polymer chains | 1 |
| Total formula weight | 8720.82 |
| Authors | Yang, F.,Varani, G. (deposition date: 2016-01-12, release date: 2016-11-23, Last modification date: 2024-05-15) |
| Primary citation | Yang, F.,Hsu, P.,Lee, S.D.,Yang, W.,Hoskinson, D.,Xu, W.,Moore, C.,Varani, G. The C terminus of Pcf11 forms a novel zinc-finger structure that plays an essential role in mRNA 3'-end processing. RNA, 23:98-107, 2017 Cited by PubMed Abstract: 3'-End processing of pre-mRNAs prior to packaging and export to the cytoplasm of the mature transcript is a highly regulated process executed by several tens of protein factors that recognize poorly conserved RNA signals. Among them is Pcf11, a highly conserved, multidomain protein that links transcriptional elongation, 3'-end processing, and transcription termination. Here we report the structure and biochemical function of Pcf11's C-terminal domain, which is conserved from yeast to humans. We identify a novel zinc-finger fold, resembling a trillium flower. Structural, biochemical, and genetic analyses reveal a highly conserved surface that plays a critical role in both cleavage and polyadenylation. These findings provide further insight into this important protein and its multiple functional roles during cotranscriptional RNA processing. PubMed: 27780845DOI: 10.1261/rna.058354.116 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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