1t1u
From Proteopedia
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| - | [[Image:1t1u.gif|left|200px]]<br /><applet load="1t1u" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1t1u, resolution 1.55Å" /> | ||
| - | '''Structural Insights and Functional Implications of Choline Acetyltransferase'''<br /> | ||
| - | == | + | ==Structural Insights and Functional Implications of Choline Acetyltransferase== |
| + | <StructureSection load='1t1u' size='340' side='right'caption='[[1t1u]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1t1u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T1U 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]] 1.55Å</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=1t1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t1u OCA], [https://pdbe.org/1t1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t1u RCSB], [https://www.ebi.ac.uk/pdbsum/1t1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t1u ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CLAT_RAT CLAT_RAT] Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses. | ||
| + | == 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/t1/1t1u_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=1t1u ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The biosynthetic enzyme for the neurotransmitter acetylcholine, choline acetyltransferase (ChAT) (E.C. 2.3.1.6), is essential for the development and neuronal activities of cholinergic systems involved in many fundamental brain functions. ChAT catalyzes the transfer of an acetyl group from acetyl-coenzyme A to choline to form the neurotransmitter acetylcholine. Since its discovery more than 60 years ago much research has been devoted to the kinetic studies of this enzyme. For the first time we report the crystal structure of rat ChAT (rChAT) to 1.55 A resolution. The structure of rChAT is a monomer and consists of two domains with an interfacial active site tunnel. This structure, with the modeled substrate binding, provides critical insights into the molecular basis for the production of acetylcholine and may further our understanding of disease causing mutations. | The biosynthetic enzyme for the neurotransmitter acetylcholine, choline acetyltransferase (ChAT) (E.C. 2.3.1.6), is essential for the development and neuronal activities of cholinergic systems involved in many fundamental brain functions. ChAT catalyzes the transfer of an acetyl group from acetyl-coenzyme A to choline to form the neurotransmitter acetylcholine. Since its discovery more than 60 years ago much research has been devoted to the kinetic studies of this enzyme. For the first time we report the crystal structure of rat ChAT (rChAT) to 1.55 A resolution. The structure of rChAT is a monomer and consists of two domains with an interfacial active site tunnel. This structure, with the modeled substrate binding, provides critical insights into the molecular basis for the production of acetylcholine and may further our understanding of disease causing mutations. | ||
| - | + | Structural insights and functional implications of choline acetyltransferase.,Govindasamy L, Pedersen B, Lian W, Kukar T, Gu Y, Jin S, Agbandje-McKenna M, Wu D, McKenna R J Struct Biol. 2004 Nov;148(2):226-35. PMID:15477102<ref>PMID:15477102</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1t1u" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Choline O-acetyltransferase|Choline O-acetyltransferase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rattus norvegicus]] | ||
| + | [[Category: Agbandje-McKenna M]] | ||
| + | [[Category: Govindasamy L]] | ||
| + | [[Category: Gu Y]] | ||
| + | [[Category: Jin S]] | ||
| + | [[Category: Kukar T]] | ||
| + | [[Category: Lian W]] | ||
| + | [[Category: Pedersen B]] | ||
| + | [[Category: Wu D]] | ||
Current revision
Structural Insights and Functional Implications of Choline Acetyltransferase
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Categories: Large Structures | Rattus norvegicus | Agbandje-McKenna M | Govindasamy L | Gu Y | Jin S | Kukar T | Lian W | Pedersen B | Wu D
