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Structure paper

TitleGAS41 promotes H2A.Z deposition through recognition of the N terminus of histone H3 by the YEATS domain.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 120, Page e2304103120-e2304103120, Year 2023
Publish dateMar 30, 2021 (structure data deposition date)
AuthorsKikuchi, M. / Takase, S. / Konuma, T. / Noritsugu, K. / Sekine, S. / Ikegami, T. / Ito, A. / Umehara, T.
External linksProc. Natl. Acad. Sci. USA / PubMed:37844223
MethodsX-ray diffraction
Resolution1.52 - 2.15 Å
Structure data

PDB-7eif:
Crystal structure of GAS41 YEATS domain
Method: X-RAY DIFFRACTION / Resolution: 1.58 Å

PDB-8iiy:
Crystal structure of MBP fused GAS41 YEATS domain in complex with H3K14ac peptide
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-8iiz:
Crystal structure of MBP fused GAS41 YEATS domain in complex with H3K27ac peptide
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-8ij0:
Crystal structure of GAS41 YEATS domain in complex with H3K9ac peptide
Method: X-RAY DIFFRACTION / Resolution: 1.52 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

Source
  • homo sapiens (human)
  • escherichia coli (E. coli)
KeywordsNUCLEAR PROTEIN / YEATS domain / Transcription / Complex / Histone modification

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