| Structural highlights
2vjd is a 2 chain structure with sequence from Torpedo californica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , |
| Related: | 1zgb, 1qti, 1amn, 1e66, 2vq6, 2j3d, 2ack, 1qii, 2ckm, 1dx6, 1qij, 1qie, 1acl, 1w4l, 1odc, 2cmf, 2j3q, 1gqs, 2j4f, 1e3q, 2dfp, 1qik, 2c5f, 1ea5, 2vjc, 1eea, 1qif, 2vjb, 1qig, 1zgc, 1qid, 1jjb, 1ut6, 2vt6, 2vt7, 2cek, 1qim, 1gpk, 1jga, 3ace, 1oce, 1w6r, 1som, 1vxo, 2vja, 1cfj, 2v96, 1ax9, 1u65, 1w76, 1h22, 1eve, 2c4h, 1gqr, 2ace, 2va9, 1vxr, 4ace, 2c58, 1hbj, 1vot, 1w75, 2c5g, 1jgb, 2v98, 1gpn, 1qih, 1h23, 1acj, 1fss, 2v97 |
| Activity: | Acetylcholinesterase, with EC number 3.1.1.7 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[ACES_TORCA] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Although x-ray crystallography is the most widely used method for macromolecular structure determination, it does not provide dynamical information, and either experimental tricks or complementary experiments must be used to overcome the inherently static nature of crystallographic structures. Here we used specific x-ray damage during temperature-controlled crystallographic experiments at a third-generation synchrotron source to trigger and monitor (Shoot-and-Trap) structural changes putatively involved in an enzymatic reaction. In particular, a nonhydrolyzable substrate analogue of acetylcholinesterase, the "off-switch" at cholinergic synapses, was radiocleaved within the buried enzymatic active site. Subsequent product clearance, observed at 150 K but not at 100 K, indicated exit from the active site possibly via a "backdoor." The simple strategy described here is, in principle, applicable to any enzyme whose structure in complex with a substrate analogue is available and, therefore, could serve as a standard procedure in kinetic crystallography studies.
Shoot-and-Trap: use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography.,Colletier JP, Bourgeois D, Sanson B, Fournier D, Sussman JL, Silman I, Weik M Proc Natl Acad Sci U S A. 2008 Aug 19;105(33):11742-7. Epub 2008 Aug 13. PMID:18701720[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Colletier JP, Bourgeois D, Sanson B, Fournier D, Sussman JL, Silman I, Weik M. Shoot-and-Trap: use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography. Proc Natl Acad Sci U S A. 2008 Aug 19;105(33):11742-7. Epub 2008 Aug 13. PMID:18701720
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