2fy2: Difference between revisions

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-{{Seed}}
-[[Image:2fy2.png|left|200px]]
-<!--
+==Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis==
-The line below this paragraph, containing "STRUCTURE_2fy2", creates the "Structure Box" on the page.
+<StructureSection load='2fy2' size='340' side='right'caption='[[2fy2]], [[Resolution|resolution]] 2.25&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'>[[2fy2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FY2 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]] 2.25&#8491;</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=2fy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fy2 OCA], [https://pdbe.org/2fy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fy2 RCSB], [https://www.ebi.ac.uk/pdbsum/2fy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fy2 ProSAT]</span></td></tr>
-{{STRUCTURE_2fy2|  PDB=2fy2  |  SCENE=  }}
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/CLAT_HUMAN CLAT_HUMAN] Defects in CHAT are the cause of congenital myasthenic syndrome with episodic apnea (CMSEA) [MIM:[https://omim.org/entry/254210 254210]; formerly known as familial infantile myasthenia gravis 2 (FIMG2). CMSEA is an autosomal recessive congenital myasthenic syndrome. Patients have myasthenic symptoms since birth or early infancy, negative tests for anti-AChR antibodies, and abrupt episodic crises with increased weakness, bulbar paralysis, and apnea precipitated by undue exertion, fever, or excitement.<ref>PMID:11172068</ref> <ref>PMID:12756141</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/CLAT_HUMAN CLAT_HUMAN] 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/fy/2fy2_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=2fy2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Choline acetyltransferase (ChAT) catalyzes the synthesis of the neurotransmitter acetylcholine from choline and acetyl-CoA, and its presence is a defining feature of cholinergic neurons. We report the structure of human ChAT to a resolution of 2.2 A along with structures for binary complexes of ChAT with choline, CoA, and a nonhydrolyzable acetyl-CoA analogue, S-(2-oxopropyl)-CoA. The ChAT-choline complex shows which features of choline are important for binding and explains how modifications of the choline trimethylammonium group can be tolerated by the enzyme. A detailed model of the ternary Michaelis complex fully supports the direct transfer of the acetyl group from acetyl-CoA to choline through a mechanism similar to that seen in the serine hydrolases for the formation of an acyl-enzyme intermediate. Domain movements accompany CoA binding, and a surface loop, which is disordered in the unliganded enzyme, becomes localized and binds directly to the phosphates of CoA, stabilizing the complex. Interactions between this surface loop and CoA may function to lower the KM for CoA and could be important for phosphorylation-dependent regulation of ChAT activity.
-===Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis===
+Substrate binding and catalytic mechanism of human choline acetyltransferase.,Kim AR, Rylett RJ, Shilton BH Biochemistry. 2006 Dec 12;45(49):14621-31. PMID:17144655<ref>PMID:17144655</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2fy2" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17144655}}, adds the Publication Abstract to the page
+*[[Choline O-acetyltransferase|Choline O-acetyltransferase]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17144655 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17144655}}
+__TOC__
+</StructureSection>
-==Disease==
-Known disease associated with this structure: Myasthenic syndrome, congenital, associated with episodic apnea OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=118490 118490]]
-==About this Structure==
-FY2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FY2 OCA].
-==Reference==
-Substrate binding and catalytic mechanism of human choline acetyltransferase., Kim AR, Rylett RJ, Shilton BH, Biochemistry. 2006 Dec 12;45(49):14621-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17144655 17144655]
-[[Category: Choline O-acetyltransferase]]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Kim, A R.]]
+[[Category: Kim AR]]
-[[Category: Rylett, R J.]]
+[[Category: Rylett RJ]]
-[[Category: Shilton, B H.]]
+[[Category: Shilton BH]]
-[[Category: Alpha-beta protein]]
-[[Category: Transferase]]
-[[Category: Two domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:45:21 2008''