1cjw: Difference between revisions

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[[Image:1cjw.gif|left|200px]]
[[Image:1cjw.png|left|200px]]


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==Overview==
{{ABSTRACT_10319816}}
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==
==About this Structure==
1CJW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJW OCA].  
1CJW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJW 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:[http://www.ncbi.nlm.nih.gov/pubmed/10319816 10319816]
[[Category: Ovis aries]]
[[Category: Ovis aries]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Namboodiri, M A.A.]]
[[Category: Namboodiri, M A.A.]]
[[Category: N-acetyl transferase]]
[[Category: N-acetyl transferase]]
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