1t1u
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(New page: 200px<br /><applet load="1t1u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t1u, resolution 1.55Å" /> '''Structural Insights ...)
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Revision as of 00:48, 21 November 2007
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Structural Insights and Functional Implications of Choline Acetyltransferase
Overview
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.
About this Structure
1T1U is a Single protein structure of sequence from Rattus norvegicus. Active as Choline O-acetyltransferase, with EC number 2.3.1.6 Full crystallographic information is available from OCA.
Reference
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
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