2c5g: Difference between revisions

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Revision as of 02:16, 31 March 2008

File:2c5g.gif

, resolution 1.95Å

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 THIOCHOLINE

OverviewOverview

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 StructureAbout this Structure

2C5G is a Single protein structure of sequence from Torpedo californica. Full crystallographic information is available from OCA.

ReferenceReference

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 02:16:36 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 4: / Line 4: @@
 |PDB= 2c5g |SIZE=350|CAPTION= <scene name='initialview01'>2c5g</scene>, resolution 1.95&Aring;
 |SITE= <scene name='pdbsite=AC1:Pig+Binding+Site+For+Chain+A'>AC1</scene>
-|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ETM:2-(TRIMETHYLAMMONIUM)ETHYL+THIOL'>ETM</scene> and <scene name='pdbligand=PGE:TRIETHYLENE GLYCOL'>PGE</scene>
+|LIGAND= <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=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=
+|DOMAIN=
+|RELATEDENTRY=
+|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c5g OCA], [http://www.ebi.ac.uk/pdbsum/2c5g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c5g RCSB]</span>
 }}
@@ Line 30: / Line 33: @@
 [[Category: Weik, M.]]
 [[Category: Zaccai, G.]]
-[[Category: CL]]
-[[Category: ETM]]
-[[Category: NAG]]
-[[Category: PGE]]
 [[Category: alpha/beta hydrolase]]
 [[Category: alternative splicing]]
@@ Line 48: / Line 47: @@
 [[Category: synapse]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:11:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:16:36 2008''