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| ATOMIC-STRUCTURE OF ACETYLCHOLINESTERASE FROM TORPEDO-CALIFORNICA - A PROTOTYPIC ACETYLCHOLINE-BINDING PROTEIN |
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| Author(s): SUSSMAN JL, HAREL M, FROLOW F, OEFNER C, GOLDMAN A, TOKER L, SILMAN I |
| Source: SCIENCE Volume: 253 Issue: 5022 Pages: 872-879 Published: AUG 23 1991 |
| Times Cited: 1,555 References: 99 |
| Abstract: The three-dimensional structure of acetylcholinesterase from Torpedo californica electric organ has been determined by x-ray analysis to 2.8 angstrom resolution. The form crystallized is the glycolipid-anchored homodimer that was purified subsequent to solubilization with a bacterial phosphatidylinositol-specific phospholipase C. The enzyme monomer is an alpha/beta-protein that contains 537 amino acids. It consists of a 12-stranded mixed beta-sheet surrounded by 14 alpha-helices and bears a striking resemblance to several hydrolase structures including dienelactone hydrolase, serine carboxypeptidase-II, three neutral lipases, and haloalkane dehalogenase. The active site is unusual because it contains Glu, not Asp, in the Ser-His-acid catalytic triad and because the relation of the triad to the rest of the protein approximates a mirror image of that seen in the serine proteases. Furthermore, the active site lies near the bottom of a deep and narrow gorge that reaches halfway into the protein. Modeling of acetylcholine binding to the enzyme suggests that the quaternary ammonium ion is bound not to a negatively charged "anionic" site, but rather to some of the 14 aromatic residues that line the |
| Document Type: Article |
| Language: English |
| Reprint Address: SUSSMAN, JL (reprint author), WEIZMANN INST SCI, DEPT STRUCT CHEM, IL-76100 REHOVOT, ISRAEL |
Addresses:
1. RUTGERS STATE UNIV, WAKSMAN INST MICROBIOL, NEW BRUNSWICK, NJ 08903 USA
2. F HOFFMANN LA ROCHE & CO LTD, CENT RES UNIT, CH-4002 BASEL, SWITZERLAND
3. WEIZMANN INST SCI, DEPT NEUROBIOL, IL-76100 REHOVOT, ISRAEL |
| Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: GC152 |
| ISSN: 0036-8075 |
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