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Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation.

Serotonin N-acetyltransferase (AANAT) controls the daily rhythm in melatonin synthesis. When isolated from tissue, AANAT copurifies with isoforms epsilon and zeta of 14-3-3. We have determined the structure of AANAT bound to 14-3-3zeta, an association that is phosphorylation dependent. AANAT is bound in the central channel of the 14-3-3zeta dimer, and is held in place by extensive interactions both with the amphipathic phosphopeptide binding groove of 14-3-3zeta and with other parts of the central channel. Thermodynamic and activity measurements, together with crystallographic analysis, indicate that binding of AANAT by 14-3-3zeta modulates AANAT's activity and affinity for its substrates by stabilizing a region of AANAT involved in substrate binding.

Pubmed ID: 11336675


  • Obsil T
  • Ghirlando R
  • Klein DC
  • Ganguly S
  • Dyda F



Publication Data

April 20, 2001

Associated Grants


Mesh Terms

  • 14-3-3 Proteins
  • Animals
  • Arylamine N-Acetyltransferase
  • Calorimetry
  • Crystallography, X-Ray
  • Genes, Reporter
  • Humans
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins
  • Sheep
  • Tyrosine 3-Monooxygenase