2c58

TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH 20MM ACETYLTHIOCHOLINETORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH 20MM ACETYLTHIOCHOLINE

Structural highlights 2c58 is a 1 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: , , , , NonStd Res: Related: 1acj, 1acl, 1amn, 1ax9, 1cfj, 1dx6, 1e3q, 1e66, 1ea5, 1eea, 1eve, 1fss, 1gpk, 1gpn, 1gqr, 1gqs, 1h22, 1h23, 1hbj, 1jga, 1jgb, 1jjb, 1oce, 1odc, 1qid, 1qie, 1qif, 1qig, 1qih, 1qii, 1qij, 1qik, 1qim, 1qti, 1som, 1u65, 1ut6, 1vot, 1vxo, 1vxr, 1w4l, 1w6r, 1w75, 1w76, 1zgb, 1zgc, 2ace, 2ack, 2c4h, 2c5f, 2c5g, 2dfp, 3ace, 4ace 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 Acetylcholinesterase (AChE) terminates nerve-impulse transmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter, acetylcholine. Substrate traffic in AChE involves at least two binding sites, the catalytic and peripheral anionic sites, which have been suggested to be allosterically related and involved in substrate inhibition. Here, we present the crystal structures of Torpedo californica AChE complexed with the substrate acetylthiocholine, the product thiocholine and a nonhydrolysable substrate analogue. These structures provide a series of static snapshots of the substrate en route to the active site and identify, for the first time, binding of substrate and product at both the peripheral and active sites. Furthermore, they provide structural insight into substrate inhibition in AChE at two different substrate concentrations. Our structural data indicate that substrate inhibition at moderate substrate concentration is due to choline exit being hindered by a substrate molecule bound at the peripheral site. At the higher concentration, substrate inhibition arises from prevention of exit of acetate due to binding of two substrate molecules within the active-site gorge. Structural insights into substrate traffic and inhibition in acetylcholinesterase.,Colletier JP, Fournier D, Greenblatt HM, Stojan J, Sussman JL, Zaccai G, Silman I, Weik M EMBO J. 2006 Jun 21;25(12):2746-56. Epub 2006 Jun 8. PMID:16763558 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also 3D structures of acetylcholinesterase

spinqualitylabelsall models 2c58, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image