1ib1

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[[Image:1ib1.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX==
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|PDB= 1ib1 |SIZE=350|CAPTION= <scene name='initialview01'>1ib1</scene>, resolution 2.7&Aring;
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<StructureSection load='1ib1' size='340' side='right'caption='[[1ib1]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=COT:COA-S-ACETYL+TRYPTAMINE'>COT</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene>
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<table><tr><td colspan='2'>[[1ib1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IB1 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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|GENE= YWHAZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), AANAT OR SNAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9940 Ovis aries])
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<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>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ib1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ib1 OCA], [https://pdbe.org/1ib1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ib1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ib1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ib1 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ib1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ib1 OCA], [http://www.ebi.ac.uk/pdbsum/1ib1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ib1 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/1ib1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ib1 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Serotonin N-acetyltransferase (AANAT) controls the daily rhythm in melatonin synthesis. When isolated from tissue, AANAT copurifies with isoforms epsilon and zeta of 14-3-3. We have determined the structure of AANAT bound to 14-3-3zeta, an association that is phosphorylation dependent. AANAT is bound in the central channel of the 14-3-3zeta dimer, and is held in place by extensive interactions both with the amphipathic phosphopeptide binding groove of 14-3-3zeta and with other parts of the central channel. Thermodynamic and activity measurements, together with crystallographic analysis, indicate that binding of AANAT by 14-3-3zeta modulates AANAT's activity and affinity for its substrates by stabilizing a region of AANAT involved in substrate binding.
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'''CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX'''
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Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation.,Obsil T, Ghirlando R, Klein DC, Ganguly S, Dyda F Cell. 2001 Apr 20;105(2):257-67. PMID:11336675<ref>PMID:11336675</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ib1" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Serotonin N-acetyltransferase (AANAT) controls the daily rhythm in melatonin synthesis. When isolated from tissue, AANAT copurifies with isoforms epsilon and zeta of 14-3-3. We have determined the structure of AANAT bound to 14-3-3zeta, an association that is phosphorylation dependent. AANAT is bound in the central channel of the 14-3-3zeta dimer, and is held in place by extensive interactions both with the amphipathic phosphopeptide binding groove of 14-3-3zeta and with other parts of the central channel. Thermodynamic and activity measurements, together with crystallographic analysis, indicate that binding of AANAT by 14-3-3zeta modulates AANAT's activity and affinity for its substrates by stabilizing a region of AANAT involved in substrate binding.
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*[[Serotonin N-acetyltransferase|Serotonin N-acetyltransferase]]
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*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
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==About this Structure==
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== References ==
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1IB1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IB1 OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation., Obsil T, Ghirlando R, Klein DC, Ganguly S, Dyda F, Cell. 2001 Apr 20;105(2):257-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11336675 11336675]
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[[Category: Aralkylamine N-acetyltransferase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Ovis aries]]
[[Category: Ovis aries]]
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[[Category: Protein complex]]
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[[Category: Dyda F]]
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[[Category: Dyda, F.]]
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[[Category: Ganguly S]]
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[[Category: Ganguly, S.]]
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[[Category: Ghirlando R]]
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[[Category: Ghirlando, R.]]
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[[Category: Klein DC]]
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[[Category: Klein, D C.]]
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[[Category: Obsil T]]
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[[Category: Obsil, T.]]
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[[Category: 14-3-3]]
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[[Category: n-acetyl transferase]]
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[[Category: phosphorylation]]
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[[Category: protein-protein complex]]
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[[Category: signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:17:11 2008''
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Current revision

CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX

PDB ID 1ib1

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