1cjw
From Proteopedia
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(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="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1cjw, resolution 1.80Å" /> | ||
| - | '''SEROTONIN N-ACETYLTRANFERASE COMPLEXED WITH A BISUBSTRATE ANALOG'''<br /> | ||
| - | == | + | ==SEROTONIN N-ACETYLTRANSFERASE COMPLEXED WITH A BISUBSTRATE ANALOG== |
| - | Serotonin N-acetyltransferase, a member of the GNAT acetyltransferase | + | <StructureSection load='1cjw' size='340' side='right'caption='[[1cjw]], [[Resolution|resolution]] 1.80Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1cjw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. The January 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Circadian Clock Proteins'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_1 10.2210/rcsb_pdb/mom_2008_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJW FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COT:COA-S-ACETYL+TRYPTAMINE'>COT</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjw OCA], [https://pdbe.org/1cjw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cjw RCSB], [https://www.ebi.ac.uk/pdbsum/1cjw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cjw 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/cj/1cjw_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=1cjw ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:10319816</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1cjw" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Serotonin N-acetyltransferase|Serotonin N-acetyltransferase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Circadian Clock Proteins]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ovis aries]] | ||
| + | [[Category: RCSB PDB Molecule of the Month]] | ||
| + | [[Category: Dyda F]] | ||
| + | [[Category: Hickman AB]] | ||
| + | [[Category: Klein DC]] | ||
| + | [[Category: Namboodiri MAA]] | ||
Current revision
SEROTONIN N-ACETYLTRANSFERASE COMPLEXED WITH A BISUBSTRATE ANALOG
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