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| | <StructureSection load='1q6x' size='340' side='right'caption='[[1q6x]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1q6x' size='340' side='right'caption='[[1q6x]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1q6x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q6X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Q6X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1q6x]] is a 2 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=1Q6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q6X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cholinergic gene locus ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Choline_O-acetyltransferase Choline O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.6 2.3.1.6] </span></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=1q6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q6x OCA], [https://pdbe.org/1q6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q6x RCSB], [https://www.ebi.ac.uk/pdbsum/1q6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q6x ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1q6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q6x OCA], [http://pdbe.org/1q6x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q6x RCSB], [http://www.ebi.ac.uk/pdbsum/1q6x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q6x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CLAT_RAT CLAT_RAT]] Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses. | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| - | [[Category: Choline O-acetyltransferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cai, Y]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Rodgers, D W]] | + | [[Category: Cai Y]] |
| - | [[Category: Alpha beta sandwich]] | + | [[Category: Rodgers DW]] |
| - | [[Category: Extended loop]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Two domain]]
| + | |
| Structural highlights
Function
CLAT_RAT Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.
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
Choline acetyltransferase (ChAT) synthesizes acetylcholine in neurons and other cell types. Decreases in ChAT activity are associated with a number of disease states, and mutations in ChAT cause congenital neuromuscular disorders. The crystal structure of ChAT reported here shows the enzyme divided into two domains with the active site in a solvent accessible tunnel at the domain interface. A low-resolution view of the complex with one substrate, coenzyme A, defines its binding site and suggests an additional interaction not found in the related carnitine acetyltransferase. Also, the preference for choline over carnitine as an acetyl acceptor is seen to result from both electrostatic and steric blocks to carnitine binding at the active site. While half of the mutations that cause motor disorders are positioned to affect enzyme activity directly, the remaining changes are surprisingly distant from the active site and must exert indirect effects. The structure indicates how ChAT is regulated by phosphorylation and reveals an unusual pattern of basic surface patches that may mediate membrane association or macromolecular interactions.
Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders.,Cai Y, Cronin CN, Engel AG, Ohno K, Hersh LB, Rodgers DW EMBO J. 2004 May 19;23(10):2047-58. Epub 2004 May 6. PMID:15131697[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cai Y, Cronin CN, Engel AG, Ohno K, Hersh LB, Rodgers DW. Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders. EMBO J. 2004 May 19;23(10):2047-58. Epub 2004 May 6. PMID:15131697 doi:10.1038/sj.emboj.7600221
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