1q6x
From Proteopedia
(New page: 200px<br /><applet load="1q6x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q6x, resolution 2.50Å" /> '''Crystal structure of...) |
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| - | [[Image:1q6x.gif|left|200px]]<br /><applet load="1q6x" size=" | + | [[Image:1q6x.gif|left|200px]]<br /><applet load="1q6x" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q6x, resolution 2.50Å" /> | caption="1q6x, resolution 2.50Å" /> | ||
'''Crystal structure of rat choline acetyltransferase'''<br /> | '''Crystal structure of rat choline acetyltransferase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Choline acetyltransferase (ChAT) synthesizes acetylcholine in neurons and | + | Choline acetyltransferase (ChAT) synthesizes acetylcholine in neurons and other cell types. Decreases in ChAT activity are associated with a number of disease states, and mutations in ChAT cause congenital neuromuscular disorders. The crystal structure of ChAT reported here shows the enzyme divided into two domains with the active site in a solvent accessible tunnel at the domain interface. A low-resolution view of the complex with one substrate, coenzyme A, defines its binding site and suggests an additional interaction not found in the related carnitine acetyltransferase. Also, the preference for choline over carnitine as an acetyl acceptor is seen to result from both electrostatic and steric blocks to carnitine binding at the active site. While half of the mutations that cause motor disorders are positioned to affect enzyme activity directly, the remaining changes are surprisingly distant from the active site and must exert indirect effects. The structure indicates how ChAT is regulated by phosphorylation and reveals an unusual pattern of basic surface patches that may mediate membrane association or macromolecular interactions. |
==About this Structure== | ==About this Structure== | ||
| - | 1Q6X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1Q6X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1Q6X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cai, Y.]] | [[Category: Cai, Y.]] | ||
| - | [[Category: Rodgers, D | + | [[Category: Rodgers, D W.]] |
[[Category: NA]] | [[Category: NA]] | ||
[[Category: alpha beta sandwich]] | [[Category: alpha beta sandwich]] | ||
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[[Category: two domains]] | [[Category: two domains]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:33 2008'' |
Revision as of 12:36, 21 February 2008
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Crystal structure of rat choline acetyltransferase
Overview
Choline acetyltransferase (ChAT) synthesizes acetylcholine in neurons and other cell types. Decreases in ChAT activity are associated with a number of disease states, and mutations in ChAT cause congenital neuromuscular disorders. The crystal structure of ChAT reported here shows the enzyme divided into two domains with the active site in a solvent accessible tunnel at the domain interface. A low-resolution view of the complex with one substrate, coenzyme A, defines its binding site and suggests an additional interaction not found in the related carnitine acetyltransferase. Also, the preference for choline over carnitine as an acetyl acceptor is seen to result from both electrostatic and steric blocks to carnitine binding at the active site. While half of the mutations that cause motor disorders are positioned to affect enzyme activity directly, the remaining changes are surprisingly distant from the active site and must exert indirect effects. The structure indicates how ChAT is regulated by phosphorylation and reveals an unusual pattern of basic surface patches that may mediate membrane association or macromolecular interactions.
About this Structure
1Q6X is a Single protein structure of sequence from Rattus norvegicus with as ligand. Active as Choline O-acetyltransferase, with EC number 2.3.1.6 Full crystallographic information is available from OCA.
Reference
Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders., Cai Y, Cronin CN, Engel AG, Ohno K, Hersh LB, Rodgers DW, EMBO J. 2004 May 19;23(10):2047-58. Epub 2004 May 6. PMID:15131697
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