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1SZ9

The RNA polymerase II CTD in mRNA processing: beta-turn recognition and beta-spiral model

Summary for 1SZ9
Entry DOI10.2210/pdb1sz9/pdb
Related1SZA
DescriptorPCF11 protein (2 entities in total)
Functional Keywordspcf11, rna polymerase ii ctd interacting domain, arm repeats, transcription
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Cellular locationNucleus : P39081
Total number of polymer chains3
Total formula weight49872.43
Authors
Meinhart, A.,Cramer, P. (deposition date: 2004-04-05, release date: 2004-07-13, Last modification date: 2024-04-03)
Primary citationMeinhart, A.,Cramer, P.
Recognition of RNA polymerase II carboxy-terminal domain by 3'-RNA-processing factors.
Nature, 430:223-226, 2004
Cited by
PubMed Abstract: During transcription, RNA polymerase (Pol) II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing by the carboxy-terminal domain (CTD) of Pol II, which consists of up to 52 repeats of the sequence Tyr 1-Ser 2-Pro 3-Thr 4-Ser 5-Pro 6-Ser 7 (refs 1, 2). After phosphorylation, the CTD binds tightly to a conserved CTD-interacting domain (CID) present in the proteins Pcf11 and Nrd1, which are essential and evolutionarily conserved factors for polyadenylation-dependent and -independent 3'-RNA processing, respectively. Here we describe the structure of a Ser 2-phosphorylated CTD peptide bound to the CID domain of Pcf11. The CTD motif Ser 2-Pro 3-Thr 4-Ser 5 forms a beta-turn that binds to a conserved groove in the CID domain. The Ser 2 phosphate group does not make direct contact with the CID domain, but may be recognized indirectly because it stabilizes the beta-turn with an additional hydrogen bond. Iteration of the peptide structure results in a compact beta-spiral model of the CTD. The model suggests that, during the mRNA transcription-processing cycle, compact spiral regions in the CTD are unravelled and regenerated in a phosphorylation-dependent manner.
PubMed: 15241417
DOI: 10.1038/nature02679
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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数据于2025-12-03公开中

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