1qo9 | pdb_00001qo9
NATIVE ACETYLCHOLINESTERASE FROM DROSOPHILA MELANOGASTER
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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
1QO9 is a Single protein structure of sequence from Drosophila melanogaster with NAG as ligand. Active as Acetylcholinesterase, with EC number 3.1.1.7 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
Page seeded by OCA on Thu Nov 8 12:42:48 2007
