1maa

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[[Image:1maa.gif|left|200px]]<br /><applet load="1maa" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1maa.gif|left|200px]]
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caption="1maa, resolution 2.9&Aring;" />
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'''MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN, GLYCOSYLATED PROTEIN'''<br />
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{{Structure
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|PDB= 1maa |SIZE=350|CAPTION= <scene name='initialview01'>1maa</scene>, resolution 2.9&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=DME:DECAMETHONIUM+ION'>DME</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7]
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|GENE= MOUSE ACHE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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}}
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'''MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN, GLYCOSYLATED PROTEIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1MAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=DME:'>DME</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAA OCA].
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1MAA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAA OCA].
==Reference==
==Reference==
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Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly., Bourne Y, Taylor P, Bougis PE, Marchot P, J Biol Chem. 1999 Jan 29;274(5):2963-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9915834 9915834]
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Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly., Bourne Y, Taylor P, Bougis PE, Marchot P, J Biol Chem. 1999 Jan 29;274(5):2963-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9915834 9915834]
[[Category: Acetylcholinesterase]]
[[Category: Acetylcholinesterase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: tetramer]]
[[Category: tetramer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:41:02 2008''

Revision as of 10:41, 20 March 2008

Image:1maa.gif


PDB ID 1maa

Drag the structure with the mouse to rotate
, resolution 2.9Å
Ligands: , , and
Gene: MOUSE ACHE (Mus musculus)
Activity: Acetylcholinesterase, with EC number 3.1.1.7
Coordinates: save as pdb, mmCIF, xml



MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN, GLYCOSYLATED PROTEIN


Overview

The crystal structure of mouse acetylcholinesterase at 2.9-A resolution reveals a tetrameric assembly of subunits with an antiparallel alignment of two canonical homodimers assembled through four-helix bundles. In the tetramer, a short Omega loop, composed of a cluster of hydrophobic residues conserved in mammalian acetylcholinesterases along with flanking alpha-helices, associates with the peripheral anionic site of the facing subunit and sterically occludes the entrance of the gorge leading to the active center. The inverse loop-peripheral site interaction occurs within the second pair of subunits, but the peripheral sites on the two loop-donor subunits remain freely accessible to the solvent. The position and complementarity of the peripheral site-occluding loop mimic the characteristics of the central loop of the peptidic inhibitor fasciculin bound to mouse acetylcholinesterase. Tetrameric forms of cholinesterases are widely distributed in nature and predominate in mammalian brain. This structure reveals a likely mode of subunit arrangement and suggests that the peripheral site, located near the rim of the gorge, is a site for association of neighboring subunits or heterologous proteins with interactive surface loops.

About this Structure

1MAA is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly., Bourne Y, Taylor P, Bougis PE, Marchot P, J Biol Chem. 1999 Jan 29;274(5):2963-70. PMID:9915834

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