2fy3: Difference between revisions
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[[Image:2fy3.gif|left|200px]] | [[Image:2fy3.gif|left|200px]] | ||
'''Structures of ligand bound human choline acetyltransferase provides insight into regulation of acetylcholine synthesis''' | {{Structure | ||
|PDB= 2fy3 |SIZE=350|CAPTION= <scene name='initialview01'>2fy3</scene>, resolution 2.27Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= [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] | |||
|GENE= CHAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Structures of ligand bound human choline acetyltransferase provides insight into regulation of acetylcholine synthesis''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2FY3 is a [ | 2FY3 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=2FY3 OCA]. | ||
==Reference== | ==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:// | 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: Choline O-acetyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: two domain]] | [[Category: two domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:58:06 2008'' | ||
Revision as of 17:58, 20 March 2008
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| , resolution 2.27Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | CHAT (Homo sapiens) | ||||||
| Activity: | Choline O-acetyltransferase, with EC number 2.3.1.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structures of ligand bound human choline acetyltransferase provides insight into regulation of acetylcholine synthesis
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Myasthenic syndrome, congenital, associated with episodic apnea OMIM:[118490]
About this StructureAbout this Structure
2FY3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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