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TitlePalmitoylated acyl protein thioesterase APT2 deforms membranes to extract substrate acyl chains.
Journal, issue, pagesNat. Chem. Biol., Year 2021
Publish dateJan 12, 2019 (structure data deposition date)
AuthorsAbrami, L. / Audagnotto, M. / Ho, S. / Marcaida, M.J. / Mesquita, F.S. / Anwar, M.U. / Sandoz, P.A. / Fonti, G. / Pojer, F. / Dal Peraro, M. / van der Goot, F.G.
External linksNat. Chem. Biol. / PubMed:33707782
MethodsX-ray diffraction
Resolution2.099 - 2.755 Å
Structure data

PDB-6qgn:
Crystal structure of APT1 bound to 2-Bromopalmitate
Method: X-RAY DIFFRACTION / Resolution: 2.099 Å

PDB-6qgo:
Crystal structure of APT1 S119A mutant bound to palmitic acid.
Method: X-RAY DIFFRACTION / Resolution: 2.599 Å

PDB-6qgq:
Crystal structure of APT1 C2S mutant bound to palmitic acid.
Method: X-RAY DIFFRACTION / Resolution: 2.601 Å

PDB-6qgs:
Crystal structure of APT1 bound to palmitic acid.
Method: X-RAY DIFFRACTION / Resolution: 2.755 Å

Chemicals

ChemComp-J1W:
2-Bromopalmitic acid

ChemComp-HOH:
WATER

ChemComp-PLM:
PALMITIC ACID

ChemComp-GOL:
GLYCEROL

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE / acyl-protein thioesterase 2-bromopalmitate Depalmitoylation / acyl-protein thioesterase / palmitic acid / Depalmitoylation

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