1maa
From Proteopedia
(New page: 200px<br /><applet load="1maa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1maa, resolution 2.9Å" /> '''MOUSE ACETYLCHOLINEST...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1maa.gif|left|200px]]<br /><applet load="1maa" size=" | + | [[Image:1maa.gif|left|200px]]<br /><applet load="1maa" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1maa, resolution 2.9Å" /> | caption="1maa, resolution 2.9Å" /> | ||
'''MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN, GLYCOSYLATED PROTEIN'''<br /> | '''MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN, GLYCOSYLATED PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of mouse acetylcholinesterase at 2.9-A resolution | + | 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== | ==About this Structure== | ||
| - | 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 NAG, PO4, DME and GOL 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:// | + | 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]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bougis, P | + | [[Category: Bougis, P E.]] |
[[Category: Bourne, Y.]] | [[Category: Bourne, Y.]] | ||
[[Category: Marchot, P.]] | [[Category: Marchot, P.]] | ||
| Line 29: | Line 29: | ||
[[Category: tetramer]] | [[Category: tetramer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:09 2008'' |
Revision as of 11:53, 21 February 2008
|
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 with , , and as ligands. Active as Acetylcholinesterase, with EC number 3.1.1.7 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
Page seeded by OCA on Thu Feb 21 13:53:09 2008
Categories: Acetylcholinesterase | Mus musculus | Single protein | Bougis, P E. | Bourne, Y. | Marchot, P. | Taylor, P. | DME | GOL | NAG | PO4 | Glycosylated protein | Hydrolase | Hydrolase fold | Serine esterase | Tetramer
