1b6b

From Proteopedia

(Difference between revisions)

Revision as of 14:35, 25 December 2014

MELATONIN BIOSYNTHESIS: THE STRUCTURE OF SEROTONIN N-ACETYLTRANSFERASE AT 2.5 A RESOLUTION SUGGESTS A CATALYTIC MECHANISM

Structural highlights

1b6b is a 2 chain structure with sequence from Ovis aries. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Aralkylamine N-acetyltransferase, with EC number 2.3.1.87
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[SNAT_SHEEP] Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ganguly S, Weller JL, Ho A, Chemineau P, Malpaux B, Klein DC. Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205. Proc Natl Acad Sci U S A. 2005 Jan 25;102(4):1222-7. Epub 2005 Jan 11. PMID:15644438 doi:0406871102
↑ Hickman AB, Klein DC, Dyda F. Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism. Mol Cell. 1999 Jan;3(1):23-32. PMID:10024876

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b6b"

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b6b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b6b RCSB], [http://www.ebi.ac.uk/pdbsum/1b6b PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SNAT_SHEEP SNAT_SHEEP]] Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin.<ref>PMID:15644438</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1b6b

From Proteopedia

Revision as of 14:35, 25 December 2014

MELATONIN BIOSYNTHESIS: THE STRUCTURE OF SEROTONIN N-ACETYLTRANSFERASE AT 2.5 A RESOLUTION SUGGESTS A CATALYTIC MECHANISM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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