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''' | + | {{Structure |
| + | |PDB= 1cjw |SIZE=350|CAPTION= <scene name='initialview01'>1cjw</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=COT:COA-S-ACETYL TRYPTAMINE'>COT</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SEROTONIN N-ACETYLTRANFERASE COMPLEXED WITH A BISUBSTRATE ANALOG''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CJW is a [ | + | 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== | ==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:// | + | 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: n-acetyl transferase]] | [[Category: n-acetyl transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:25:19 2008'' |
Revision as of 08:25, 20 March 2008
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| , resolution 1.80Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 10:25:19 2008
