Cell. 2001 Apr 20;105(2):257-67.

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

Obsil T, Ghirlando R, Klein DC, Ganguly S, Dyda F.

Source

Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Abstract

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.

PMID:: 11336675; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Crystal Structure Of The 14-3-3 Zeta:serotonin N- Acetyltransferase Complex

PDB: 1IB1

Source: Homo sapiens, Ovis aries

Method: X-Ray Diffraction

Resolution: 2.7 Å

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