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 1.55&Aring;" /> '''Structural Insights ...)
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[[Image:1t1u.gif|left|200px]]<br /><applet load="1t1u" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1t1u, resolution 1.55&Aring;" />
caption="1t1u, resolution 1.55&Aring;" />
'''Structural Insights and Functional Implications of Choline Acetyltransferase'''<br />
'''Structural Insights and Functional Implications of Choline Acetyltransferase'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1T1U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T1U OCA].
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1T1U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1U OCA].
==Reference==
==Reference==
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[[Category: choline acetyltransferase]]
[[Category: choline acetyltransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:55:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:59 2008''

Revision as of 13:09, 21 February 2008


1t1u, resolution 1.55Å

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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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