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[[Image:1kuv.jpg|left|200px]]


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==X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition==
The line below this paragraph, containing "STRUCTURE_1kuv", creates the "Structure Box" on the page.
<StructureSection load='1kuv' size='340' side='right'caption='[[1kuv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1kuv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KUV FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA5:COA-S-ACETYL+5-BROMOTRYPTAMINE'>CA5</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_1kuv| PDB=1kuv |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kuv OCA], [https://pdbe.org/1kuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kuv RCSB], [https://www.ebi.ac.uk/pdbsum/1kuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kuv ProSAT]</span></td></tr>
</table>
== Function ==
[https://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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ku/1kuv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kuv ConSurf].
<div style="clear:both"></div>


'''X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition'''
==See Also==
 
*[[Serotonin N-acetyltransferase|Serotonin N-acetyltransferase]]
 
== References ==
==Overview==
<references/>
The structure of serotonin N-acetyltransferase (also known as arylalkylamine N-acetyltransferase; AANAT) bound to a potent bisubstrate analog inhibitor has been determined at 2.0 A resolution using a two-edge (Se, Br) multiwavelength anomalous diffraction (MAD) experiment. This acetyl-CoA dependent enzyme is a member of the GCN5-related family of N-acetyltransferases (GNATs), which share four conserved sequence motifs (A-D). In serotonin N-acetyltransferase, motif A adopts an alpha/beta conformation characteristic of the phylogenetically invariant cofactor binding site seen in all previously characterized GNATs. Motif B displays a significantly lower level of conservation among family members, giving rise to a novel alpha/beta structure for the serotonin binding slot. Utilization of a brominated CoA-S-acetyl-tryptamine-bisubstrate analog inhibitor and the MAD method permitted conclusive identification of two radically different conformations for the tryptamine moiety in the catalytic site (cis and trans). A second high-resolution X-ray structure of the enzyme bound to a bisubstrate analog inhibitor, with a longer tether between the acetyl-CoA and tryptamine moieties, demonstrates only the trans conformation. Given a previous proposal that AANAT can catalyze an alkyltransferase reaction in a conformationally altered active site relative to its acetyltransferase activity, it is possible that the two conformations of the bisubstrate analog observed crystallographically correspond to these alternative reaction pathways. Our findings may ultimately lead to the design of analogs with improved AANAT inhibitory properties for in vivo applications.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1KUV 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=1KUV OCA].
 
==Reference==
X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition., Wolf E, De Angelis J, Khalil EM, Cole PA, Burley SK, J Mol Biol. 2002 Mar 22;317(2):215-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11902838 11902838]
[[Category: Aralkylamine N-acetyltransferase]]
[[Category: Ovis aries]]
[[Category: Ovis aries]]
[[Category: Single protein]]
[[Category: Burley SK]]
[[Category: Angelis, J De.]]
[[Category: Cole PA]]
[[Category: Burley, S K.]]
[[Category: De Angelis J]]
[[Category: Cole, P A.]]
[[Category: Khalil EM]]
[[Category: Khalil, E M.]]
[[Category: Wolf E]]
[[Category: Wolf, E.]]
[[Category: Alternate conformation]]
[[Category: Bisubstrate analog]]
[[Category: Enzyme-inhibitor complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:11:37 2008''

Latest revision as of 10:27, 14 February 2024

X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and InhibitionX-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition

Structural highlights

1kuv is a 1 chain structure with sequence from Ovis aries. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

  1. ↑ 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

1kuv, resolution 2.00Å

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