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Structure paper

TitleA unique surface on Pat1 C-terminal domain directly interacts with Dcp2 decapping enzyme and Xrn1 5'-3' mRNA exonuclease in yeast.
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 114, Page E9493-E9501, Year 2017
Publish dateJul 29, 2016 (structure data deposition date)
AuthorsCharenton, C. / Gaudon-Plesse, C. / Fourati, Z. / Taverniti, V. / Back, R. / Kolesnikova, O. / Seraphin, B. / Graille, M.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:29078363
MethodsX-ray diffraction
Resolution1.89 - 2.6 Å
Structure data

PDB-5lm5:
Structure of C-terminal domain from S. cerevisiae Pat1 decapping activator bound to Dcp2 HLM2 peptide (region 435-451)
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-5lmf:
Structure of C-terminal domain from S. cerevisiae Pat1 decapping activator bound to Dcp2 HLM3 peptide (region 484-500)
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-5lmg:
Structure of C-terminal domain from S. cerevisiae Pat1 decapping activator bound to Dcp2 HLM10 peptide (region 954-970)
Method: X-RAY DIFFRACTION / Resolution: 1.89 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsRNA BINDING PROTEIN / Protein peptide complex / ISOMERASE

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