1q6x

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|PDB= 1q6x |SIZE=350|CAPTION= <scene name='initialview01'>1q6x</scene>, resolution 2.50&Aring;
|PDB= 1q6x |SIZE=350|CAPTION= <scene name='initialview01'>1q6x</scene>, resolution 2.50&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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|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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE= cholinergic gene locus ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
|GENE= cholinergic gene locus ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q6x OCA], [http://www.ebi.ac.uk/pdbsum/1q6x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q6x RCSB]</span>
}}
}}
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[[Category: Cai, Y.]]
[[Category: Cai, Y.]]
[[Category: Rodgers, D W.]]
[[Category: Rodgers, D W.]]
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[[Category: NA]]
 
[[Category: alpha beta sandwich]]
[[Category: alpha beta sandwich]]
[[Category: extended loop]]
[[Category: extended loop]]
[[Category: two domain]]
[[Category: two domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:33:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:09:41 2008''

Revision as of 20:09, 30 March 2008


PDB ID 1q6x

Drag the structure with the mouse to rotate
, resolution 2.50Å
Ligands:
Gene: cholinergic gene locus (Rattus norvegicus)
Activity: Choline O-acetyltransferase, with EC number 2.3.1.6
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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