1cjw
From Proteopedia
(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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| - | [[Image:1cjw.gif|left|200px]]<br /><applet load="1cjw" size=" | + | [[Image:1cjw.gif|left|200px]]<br /><applet load="1cjw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cjw, resolution 1.80Å" /> | caption="1cjw, resolution 1.80Å" /> | ||
'''SEROTONIN N-ACETYLTRANFERASE COMPLEXED WITH A BISUBSTRATE ANALOG'''<br /> | '''SEROTONIN N-ACETYLTRANFERASE COMPLEXED WITH A BISUBSTRATE ANALOG'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Serotonin N-acetyltransferase, a member of the GNAT acetyltransferase | + | 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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] with COT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1CJW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] with <scene name='pdbligand=COT:'>COT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dyda, F.]] | [[Category: Dyda, F.]] | ||
| - | [[Category: Hickman, A | + | [[Category: Hickman, A B.]] |
| - | [[Category: Klein, D | + | [[Category: Klein, D C.]] |
| - | [[Category: Namboodiri, M | + | [[Category: Namboodiri, M A.A.]] |
[[Category: COT]] | [[Category: COT]] | ||
[[Category: n-acetyl transferase]] | [[Category: n-acetyl transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:01 2008'' |
Revision as of 10:07, 21 February 2008
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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 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
Page seeded by OCA on Thu Feb 21 12:07:01 2008
