Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5022
|
| pubmed:dateCreated |
1991-9-25
|
| pubmed:abstractText |
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 gorge.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholinesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamates,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0036-8075
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
23
|
| pubmed:volume |
253
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
872-9
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:1678899-Acetylcholine,
pubmed-meshheading:1678899-Acetylcholinesterase,
pubmed-meshheading:1678899-Amino Acid Sequence,
pubmed-meshheading:1678899-Animals,
pubmed-meshheading:1678899-Binding Sites,
pubmed-meshheading:1678899-Cell Membrane,
pubmed-meshheading:1678899-Chemistry, Physical,
pubmed-meshheading:1678899-Crystallization,
pubmed-meshheading:1678899-Electric Organ,
pubmed-meshheading:1678899-Glutamates,
pubmed-meshheading:1678899-Glutamic Acid,
pubmed-meshheading:1678899-Macromolecular Substances,
pubmed-meshheading:1678899-Molecular Sequence Data,
pubmed-meshheading:1678899-Molecular Structure,
pubmed-meshheading:1678899-Phosphatidylinositols,
pubmed-meshheading:1678899-Physicochemical Phenomena,
pubmed-meshheading:1678899-Protein Conformation,
pubmed-meshheading:1678899-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1678899-Torpedo,
pubmed-meshheading:1678899-X-Ray Diffraction
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.
|
| pubmed:affiliation |
Department of Structural Chemistry, Weizmann Institute of Science, Rehovot, Israel.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|