1oce
From Proteopedia
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[[Category: serine esterase]] | [[Category: serine esterase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:49:36 2007'' |
Revision as of 13:44, 30 October 2007
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ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH MF268
Overview
The crystal structure of Torpedo californica (Tc) acetylcholinesterase, (AChE) carbamoylated by the physostigmine analogue, 8-(cis-2,6-dimethylmorpholino)octylcarbamoyleseroline (MF268) is reported, at 2.7 A resolution. In the X-ray structure, the, dimethylmorpholinooctylcarbamic moiety of MF268 is covalently bound to the, catalytic serine, which is located at the bottom of a long and narrow, gorge. The alkyl chain of the inhibitor fills the upper part of the gorge, blocking the entrance of the active site. This prevents eseroline, the, leaving group of the carbamoylation process, from exiting through this, path. Surprisingly, the relatively bulky eseroline is not found in the, crystal structure, thus implying the existence of an alternative route for, its clearance. This represents ... [(full description)]
About this Structure
1OCE is a [Single protein] structure of sequence from [Torpedo californica] with MF2 as [ligand]. Active as [Acetylcholinesterase], with EC number [3.1.1.7]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
"Back door" opening implied by the crystal structure of a carbamoylated acetylcholinesterase., Bartolucci C, Perola E, Cellai L, Brufani M, Lamba D, Biochemistry. 1999 May 4;38(18):5714-9. PMID:10231521
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