1b6b
From Proteopedia
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| - | [[Image:1b6b.gif|left|200px]] | + | [[Image:1b6b.gif|left|200px]] |
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| - | '''MELATONIN BIOSYNTHESIS: THE STRUCTURE OF SEROTONIN N-ACETYLTRANSFERASE AT 2.5 A RESOLUTION SUGGESTS A CATALYTIC MECHANISM''' | + | {{Structure |
| + | |PDB= 1b6b |SIZE=350|CAPTION= <scene name='initialview01'>1b6b</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Aralkylamine_N-acetyltransferase Aralkylamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.87 2.3.1.87] | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''MELATONIN BIOSYNTHESIS: THE STRUCTURE OF SEROTONIN N-ACETYLTRANSFERASE AT 2.5 A RESOLUTION SUGGESTS A CATALYTIC MECHANISM''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1B6B is a [ | + | 1B6B 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=1B6B OCA]. |
==Reference== | ==Reference== | ||
| - | Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism., Hickman AB, Klein DC, Dyda F, Mol Cell. 1999 Jan;3(1):23-32. PMID:[http:// | + | Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism., Hickman AB, Klein DC, Dyda F, Mol Cell. 1999 Jan;3(1):23-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10024876 10024876] |
[[Category: Aralkylamine N-acetyltransferase]] | [[Category: Aralkylamine N-acetyltransferase]] | ||
[[Category: Ovis aries]] | [[Category: Ovis aries]] | ||
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[[Category: acetyltransferase]] | [[Category: acetyltransferase]] | ||
| - | ''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 10:06:51 2008'' |
Revision as of 08:06, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Activity: | Aralkylamine N-acetyltransferase, with EC number 2.3.1.87 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MELATONIN BIOSYNTHESIS: THE STRUCTURE OF SEROTONIN N-ACETYLTRANSFERASE AT 2.5 A RESOLUTION SUGGESTS A CATALYTIC MECHANISM
Overview
Conversion of serotonin to N-acetylserotonin, the precursor of the circadian neurohormone melatonin, is catalyzed by serotonin N-acetyltransferase (AANAT) in a reaction requiring acetyl coenzyme A (AcCoA). AANAT is a globular protein consisting of an eight-stranded beta sheet flanked by five alpha helices; a conserved motif in the center of the beta sheet forms the cofactor binding site. Three polypeptide loops converge above the AcCoA binding site, creating a hydrophobic funnel leading toward the cofactor and serotonin binding sites in the protein interior. Two conserved histidines not found in other NATs are located at the bottom of the funnel in the active site, suggesting a catalytic mechanism for acetylation involving imidazole groups acting as general acid/base catalysts.
About this Structure
1B6B is a Single protein structure of sequence from Ovis aries. Full crystallographic information is available from OCA.
Reference
Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism., Hickman AB, Klein DC, Dyda F, Mol Cell. 1999 Jan;3(1):23-32. PMID:10024876
Page seeded by OCA on Thu Mar 20 10:06:51 2008
