1cjw
From Proteopedia
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[[Image:1cjw.gif|left|200px]] | [[Image:1cjw.gif|left|200px]] | ||
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'''SEROTONIN N-ACETYLTRANFERASE COMPLEXED WITH A BISUBSTRATE ANALOG''' | '''SEROTONIN N-ACETYLTRANFERASE COMPLEXED WITH A BISUBSTRATE ANALOG''' | ||
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[[Category: Klein, D C.]] | [[Category: Klein, D C.]] | ||
[[Category: Namboodiri, M A.A.]] | [[Category: Namboodiri, M A.A.]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 09:48, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 12:48:53 2008