1oce
From Proteopedia
(New page: 200px<br /> <applet load="1oce" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oce, resolution 2.70Å" /> '''ACETYLCHOLINESTERAS...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1OCE is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]] with MF2 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OCE OCA]]. | + | 1OCE is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]] with MF2 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OCE OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10231521 10231521] | "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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10231521 10231521] | ||
| + | [[Category: Acetylcholinesterase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Torpedo californica]] | [[Category: Torpedo californica]] | ||
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[[Category: serine esterase]] | [[Category: serine esterase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:33:17 2007'' |
Revision as of 12:28, 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
Page seeded by OCA on Tue Oct 30 14:33:17 2007
