2c58
From Proteopedia
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|PDB= 2c58 |SIZE=350|CAPTION= <scene name='initialview01'>2c58</scene>, resolution 2.30Å | |PDB= 2c58 |SIZE=350|CAPTION= <scene name='initialview01'>2c58</scene>, resolution 2.30Å | ||
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AT3:ACETYLTHIOCHOLINE'>AT3</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ETM:2-(TRIMETHYLAMMONIUM)ETHYL+THIOL'>ETM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OAS:O-ACETYLSERINE'>OAS</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c58 OCA], [http://www.ebi.ac.uk/pdbsum/2c58 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c58 RCSB]</span> | ||
}} | }} | ||
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[[Category: Weik, M.]] | [[Category: Weik, M.]] | ||
[[Category: Zaccai, G.]] | [[Category: Zaccai, G.]] | ||
| - | [[Category: AT3]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: ETM]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: PGE]] | ||
[[Category: alpha/beta hydrolase]] | [[Category: alpha/beta hydrolase]] | ||
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
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[[Category: synapse]] | [[Category: synapse]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:16:30 2008'' |
Revision as of 23:16, 30 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , , | ||||||
| Activity: | Acetylcholinesterase, with EC number 3.1.1.7 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH 20MM ACETYLTHIOCHOLINE
Overview
Acetylcholinesterase (AChE) terminates nerve-impulse transmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter, acetylcholine. Substrate traffic in AChE involves at least two binding sites, the catalytic and peripheral anionic sites, which have been suggested to be allosterically related and involved in substrate inhibition. Here, we present the crystal structures of Torpedo californica AChE complexed with the substrate acetylthiocholine, the product thiocholine and a nonhydrolysable substrate analogue. These structures provide a series of static snapshots of the substrate en route to the active site and identify, for the first time, binding of substrate and product at both the peripheral and active sites. Furthermore, they provide structural insight into substrate inhibition in AChE at two different substrate concentrations. Our structural data indicate that substrate inhibition at moderate substrate concentration is due to choline exit being hindered by a substrate molecule bound at the peripheral site. At the higher concentration, substrate inhibition arises from prevention of exit of acetate due to binding of two substrate molecules within the active-site gorge.
About this Structure
2C58 is a Single protein structure of sequence from Torpedo californica. Full crystallographic information is available from OCA.
Reference
Structural insights into substrate traffic and inhibition in acetylcholinesterase., Colletier JP, Fournier D, Greenblatt HM, Stojan J, Sussman JL, Zaccai G, Silman I, Weik M, EMBO J. 2006 Jun 21;25(12):2746-56. Epub 2006 Jun 8. PMID:16763558
Page seeded by OCA on Mon Mar 31 02:16:30 2008
Categories: Acetylcholinesterase | Single protein | Torpedo californica | Colletier, J P. | Fournier, D. | Greenblatt, H M. | Silman, I. | Sussman, J L. | Weik, M. | Zaccai, G. | Alpha/beta hydrolase | Alternative splicing | Glycoprotein | Gpi-anchor | Hydrolase | Lipoprotein | Membrane | Neurotransmitter cleavage | Neurotransmitter degradation | Serine esterase | Substrate inhibition | Synapse
