1cjw
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(New page: 200px<br /><applet load="1cjw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cjw, resolution 1.80Å" /> '''SEROTONIN N-ACETYLTR...)
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Revision as of 10:24, 20 November 2007
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SEROTONIN N-ACETYLTRANFERASE COMPLEXED WITH A BISUBSTRATE ANALOG
Overview
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.
About this Structure
1CJW is a Single protein structure of sequence from Ovis aries with COT as ligand. Full crystallographic information is available from OCA.
Reference
The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog., Hickman AB, Namboodiri MA, Klein DC, Dyda F, Cell. 1999 Apr 30;97(3):361-9. PMID:10319816
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