Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4PN1

Structure of S. pombe Pct1 RNA triphosphatase in complex with the Spt5 CTD

Summary for 4PN1
Entry DOI10.2210/pdb4pn1/pdb
Related4PN0
DescriptormRNA-capping enzyme subunit beta, Synthetic peptide, FORMIC ACID, ... (5 entities in total)
Functional Keywordsmrna triphosphatase, hydrolase, polynucleotide 5' triphosphatase, mrna processing, mrna capping, dimer, transcription elongation factor, hydrolase-transcription regulator complex, hydrolase/transcription regulator
Biological sourceSchizosaccharomyces pombe (Fission yeast)
More
Total number of polymer chains8
Total formula weight150369.59
Authors
Lima, C.D.,Doamekpor, S.K. (deposition date: 2014-05-22, release date: 2014-11-12, Last modification date: 2023-09-27)
Primary citationDoamekpor, S.K.,Schwer, B.,Sanchez, A.M.,Shuman, S.,Lima, C.D.
Fission yeast RNA triphosphatase reads an Spt5 CTD code.
Rna, 21:113-123, 2015
Cited by
PubMed Abstract: mRNA capping enzymes are directed to nascent RNA polymerase II (Pol2) transcripts via interactions with the carboxy-terminal domains (CTDs) of Pol2 and transcription elongation factor Spt5. Fission yeast RNA triphosphatase binds to the Spt5 CTD, comprising a tandem repeat of nonapeptide motif TPAWNSGSK. Here we report the crystal structure of a Pct1·Spt5-CTD complex, which revealed two CTD docking sites on the Pct1 homodimer that engage TPAWN segments of the motif. Each Spt5 CTD interface, composed of elements from both subunits of the homodimer, is dominated by van der Waals contacts from Pct1 to the tryptophan of the CTD. The bound CTD adopts a distinctive conformation in which the peptide backbone makes a tight U-turn so that the proline stacks over the tryptophan. We show that Pct1 binding to Spt5 CTD is antagonized by threonine phosphorylation. Our results fortify an emerging concept of an "Spt5 CTD code" in which (i) the Spt5 CTD is structurally plastic and can adopt different conformations that are templated by particular cellular Spt5 CTD receptor proteins; and (ii) threonine phosphorylation of the Spt5 CTD repeat inscribes a binary on-off switch that is read by diverse CTD receptors, each in its own distinctive manner.
PubMed: 25414009
DOI: 10.1261/rna.048181.114
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.803 Å)
Structure validation

227111

数据于2024-11-06公开中

PDB statisticsPDBj update infoContact PDBjnumon