1CJW

SEROTONIN N-ACETYLTRANSFERASE COMPLEXED WITH A BISUBSTRATE ANALOG

Summary for 1CJW

• Entry DOI: 10.2210/pdb1cjw/pdb
• Descriptor: PROTEIN (SEROTONIN N-ACETYLTRANSFERASE), COA-S-ACETYL TRYPTAMINE (3 entities in total)
• Functional Keywords: n-acetyl transferase, transferase
• Biological source: Ovis aries (sheep)
• Cellular location: Cytoplasm (By similarity): Q29495
• Total number of polymer chains: 1
• Total formula weight: 19602.15

Authors

Hickman, A.B.,Namboodiri, M.A.A.,Klein, D.C.,Dyda, F. (deposition date: 1999-04-19, release date: 1999-05-06, Last modification date: 2023-08-09)

Primary citation

Hickman, A.B.,Namboodiri, M.A.,Klein, D.C.,Dyda, F.
The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog.
Cell(Cambridge,Mass.), 97:361-369, 1999

PubMed Abstract: Serotonin N-acetyltransferase, a member of the GNAT acetyltransferase superfamily, is the penultimate enzyme in the conversion of serotonin to melatonin, the circadian neurohormone. Comparison of the structures of the substrate-free enzyme and the complex with a bisubstrate analog, coenzyme A-S-acetyltryptamine, demonstrates that acetyl coenzyme A (AcCoA) binding is accompanied by a large conformational change that in turn leads to the formation of the serotonin-binding site. The structure of the complex also provides insight into how the enzyme may facilitate acetyl transfer. A water-filled channel leading from the active site to the surface provides a pathway for proton removal following amine deprotonation. Furthermore, structural and mutagenesis results indicate an important role for Tyr-168 in catalysis.

PubMed: 10319816
DOI: 10.1016/S0092-8674(00)80745-X

Experimental method

X-RAY DIFFRACTION (1.8 Å)