1JJB
A neutral molecule in cation-binding site: Specific binding of PEG-SH to Acetylcholinesterase from Torpedo californica
Summary for 1JJB
| Entry DOI | 10.2210/pdb1jjb/pdb |
| Related | 1VXR 2ACE |
| Descriptor | ACETYLCHOLINESTERASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, 1-DEOXY-1-THIO-HEPTAETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | peg (polyethylene), serine hydrolase, alpha/beta hydrolase, neurotransmitter cleavage, catalytic triad, glycosylated protein, hydrolase |
| Biological source | Torpedo californica (Pacific electric ray) |
| Cellular location | Isoform H: Cell membrane; Lipid-anchor, GPI- anchor. Isoform T: Cell membrane; Peripheral membrane protein: P04058 |
| Total number of polymer chains | 1 |
| Total formula weight | 60978.84 |
| Authors | Koellner, G.,Steiner, T.,Millard, C.B.,Silman, I.,Sussman, J.L. (deposition date: 2001-07-04, release date: 2002-07-17, Last modification date: 2024-11-20) |
| Primary citation | Koellner, G.,Steiner, T.,Millard, C.B.,Silman, I.,Sussman, J.L. A neutral molecule in a cation-binding site: specific binding of a PEG-SH to acetylcholinesterase from Torpedo californica. J.Mol.Biol., 320:721-725, 2002 Cited by PubMed Abstract: The crystal structure of acetylcholinesterase from Torpedo californica complexed with the uncharged inhibitor, PEG-SH-350 (containing mainly heptameric polyethylene glycol with a terminal thiol group) is determined at 2.3 A resolution. This is an untypical acetylcholinesterase inhibitor, since it lacks the cationic moiety typical of the substrate (acetylcholine). In the crystal structure, the elongated ligand extends along the whole of the deep and narrow active-site gorge, with the terminal thiol group bound near the bottom, close to the catalytic site. Unexpectedly, the cation-binding site (formed by the faces of aromatic side-chains) is occupied by CH(2) groups of the inhibitor, which are engaged in C-H...pi interactions that structurally mimic the cation-pi interactions made by the choline moiety of acetylcholine. In addition, the PEG-SH molecule makes numerous other weak but specific interactions of the C-H...O and C-H...pi types. PubMed: 12095250DOI: 10.1016/S0022-2836(02)00475-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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