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1dx4

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|PDB= 1dx4 |SIZE=350|CAPTION= <scene name='initialview01'>1dx4</scene>, resolution 2.7&Aring;
|PDB= 1dx4 |SIZE=350|CAPTION= <scene name='initialview01'>1dx4</scene>, resolution 2.7&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=760:9-(3-PHENYLMETHYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE'>760</scene>
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|LIGAND= <scene name='pdbligand=760:9-(3-PHENYLMETHYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE'>760</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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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|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=
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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=1dx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dx4 OCA], [http://www.ebi.ac.uk/pdbsum/1dx4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dx4 RCSB]</span>
}}
}}
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[[Category: Silman, I.]]
[[Category: Silman, I.]]
[[Category: Sussman, J L.]]
[[Category: Sussman, J L.]]
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[[Category: 760]]
 
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[[Category: NAG]]
 
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[[Category: SO4]]
 
[[Category: alternative splicing]]
[[Category: alternative splicing]]
[[Category: glycoprotein]]
[[Category: glycoprotein]]
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[[Category: synapse]]
[[Category: synapse]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:45:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:50:32 2008''

Revision as of 16:50, 30 March 2008

Image:1dx4.gif


PDB ID 1dx4

Drag the structure with the mouse to rotate
, resolution 2.7Å
Ligands: , , , ,
Activity: Acetylcholinesterase, with EC number 3.1.1.7
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



ACHE FROM DROSOPHILA MELANOGASTER COMPLEX WITH TACRINE DERIVATIVE 9-(3-PHENYLMETHYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE


Overview

We have crystallized Drosophila melanogaster acetylcholinesterase and solved the structure of the native enzyme and of its complexes with two potent reversible inhibitors, 1,2,3,4-tetrahydro-N-(phenylmethyl)-9-acridinamine and 1,2,3,4-tetrahydro-N-(3-iodophenyl-methyl)-9-acridinamine--all three at 2.7 A resolution. The refined structure of D. melanogaster acetylcholinesterase is similar to that of vertebrate acetylcholinesterases, for example, human, mouse, and fish, in its overall fold, charge distribution, and deep active-site gorge, but some of the surface loops deviate by up to 8 A from their position in the vertebrate structures, and the C-terminal helix is shifted substantially. The active-site gorge of the insect enzyme is significantly narrower than that of Torpedo californica AChE, and its trajectory is shifted several angstroms. The volume of the lower part of the gorge of the insect enzyme is approximately 50% of that of the vertebrate enzyme. Upon binding of either of the two inhibitors, nine aromatic side chains within the active-site gorge change their conformation so as to interact with the inhibitors. Some differences in activity and specificity between the insect and vertebrate enzymes can be explained by comparison of their three-dimensional structures.

About this Structure

1DX4 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors., Harel M, Kryger G, Rosenberry TL, Mallender WD, Lewis T, Fletcher RJ, Guss JM, Silman I, Sussman JL, Protein Sci. 2000 Jun;9(6):1063-72. PMID:10892800

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