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Structure paper

TitleStructural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106.
Journal, issue, pagesNature, Vol. 483, Page 104-107, Year 2012
Publish dateAug 4, 2011 (structure data deposition date)
AuthorsSu, D. / Hu, Q. / Li, Q. / Thompson, J.R. / Cui, G. / Fazly, A. / Davies, B.A. / Botuyan, M.V. / Zhang, Z. / Mer, G.
External linksNature / PubMed:22307274
MethodsNMR (solution) / X-ray diffraction
Resolution1.432 - 2.589 Å
Structure data

PDB-2lh0:
NMR structure of the histone-interacting N-terminal homodimeric region of Rtt106
Method: SOLUTION NMR

PDB-3fss:
Structure of the tandem PH domains of Rtt106
Method: X-RAY DIFFRACTION / Resolution: 1.432 Å

PDB-3tvv:
Structure of the tandem PH domains of Rtt106 (residues 68-315)
Method: X-RAY DIFFRACTION / Resolution: 2.589 Å

PDB-3tw1:
Structure of Rtt106-AHN
Method: X-RAY DIFFRACTION / Resolution: 1.772 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-MLA:
MALONIC ACID

ChemComp-HOH:
WATER

ChemComp-AHN:
N-[2-(1H-IMIDAZOL-4-YL)ETHYL]ACETAMIDE

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsCHAPERONE / HISTONE CHAPERONE / CHROMOSOMAL PROTEIN / NUCLEUS / PHOSPHOPROTEIN / TRANSCRIPTION / TRANSCRIPTION REGULATION / TRANSPOSITION / tandem pleckstrin-homology domains

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