1IB1

CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX

Summary for 1IB1

• Entry DOI: 10.2210/pdb1ib1/pdb
• Descriptor: 14-3-3 ZETA ISOFORM, SEROTONIN N-ACETYLTRANSFERASE, COA-S-ACETYL TRYPTAMINE, ... (4 entities in total)
• Functional Keywords: n-acetyl transferase, 14-3-3, signal transduction, protein-protein complex, phosphorylation, signaling protein-transferase complex, signaling protein/transferase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : P63104 Q29495
• Total number of polymer chains: 8
• Total formula weight: 204069.45

Authors

Obsil, T.,Ghirlando, R.,Klein, D.C.,Ganguly, S.,Dyda, F. (deposition date: 2001-03-26, release date: 2001-05-02, Last modification date: 2023-08-09)

Primary citation

Obsil, T.,Ghirlando, R.,Klein, D.C.,Ganguly, S.,Dyda, F.
Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation.
Cell(Cambridge,Mass.), 105:257-267, 2001

PubMed 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.

PubMed: 11336675
DOI: 10.1016/S0092-8674(01)00316-6

Experimental method

X-RAY DIFFRACTION (2.7 Å)