Structural insights and functional implications of choline acetyltransferase
| Autor: | Donghai Wu, Wei Lian, Thomas Kukar, Mavis Agbandje-McKenna, Robert McKenna, Brenda Pedersen, Yunrong Gu, Lakshmanan Govindasamy, Shouguang Jin |
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| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Protein Conformation Swine Molecular Sequence Data Crystallography X-Ray Catalysis Choline O-Acetyltransferase chemistry.chemical_compound Mice Structural Biology medicine Choline Transferase Animals Humans Coenzyme A Amino Acid Sequence Binding site Neurotransmitter Caenorhabditis elegans Binding Sites biology Sequence Homology Amino Acid Temperature Active site Choline acetyltransferase Acetylcholine Protein Structure Tertiary Rats Kinetics Biochemistry chemistry Models Chemical Mutation biology.protein Cholinergic medicine.drug |
| Zdroj: | Journal of structural biology. 148(2) |
| ISSN: | 1047-8477 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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