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Structure paper

TitleModulation of the substrate preference of a MYST acetyltransferase by a scaffold protein.
Journal, issue, pagesJ. Biol. Chem., Vol. 301, Page 108262-108262, Year 2025
Publish dateOct 16, 2024 (structure data deposition date)
AuthorsSengupta, R.N. / Brodsky, O. / Bingham, P. / Diehl, W.C. / Ferre, R. / Greasley, S.E. / Johnson, E. / Kraus, M. / Lieberman, W. / Meier, J.L. ...Sengupta, R.N. / Brodsky, O. / Bingham, P. / Diehl, W.C. / Ferre, R. / Greasley, S.E. / Johnson, E. / Kraus, M. / Lieberman, W. / Meier, J.L. / Paul, T.A. / Maegley, K.A.
External linksJ. Biol. Chem. / PubMed:39909374
MethodsX-ray diffraction
Resolution1.724 Å
Structure data

PDB-9dzn:
KAT6A MYST domain complexed with a H3K14-CoA bisubstrate inhibitor
Method: X-RAY DIFFRACTION / Resolution: 1.724 Å

Chemicals

ChemComp-CMC:
CARBOXYMETHYL COENZYME *A

ChemComp-ZN:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsTRANSFERASE/INHIBITOR / Acetylation / histone acetyltransferases / multiprotein complexes / TRANSFERASE / TRANSFERASE-INHIBITOR complex

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