2j4f
From Proteopedia
(New page: 200px<br /> <applet load="2j4f" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j4f, resolution 2.8Å" /> '''TORPEDO ACETYLCHOLIN...) |
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==About this Structure== | ==About this Structure== | ||
- | 2J4F 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 HG 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=2J4F OCA]]. | + | 2J4F 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 HG 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: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J4F OCA]]. |
==Reference== | ==Reference== | ||
A metastable state of Torpedo californica acetylcholinesterase generated by modification with organomercurials., Kreimer DI, Dolginova EA, Raves M, Sussman JL, Silman I, Weiner L, Biochemistry. 1994 Dec 6;33(48):14407-18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7981200 7981200] | A metastable state of Torpedo californica acetylcholinesterase generated by modification with organomercurials., Kreimer DI, Dolginova EA, Raves M, Sussman JL, Silman I, Weiner L, Biochemistry. 1994 Dec 6;33(48):14407-18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7981200 7981200] | ||
+ | [[Category: Acetylcholinesterase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Torpedo californica]] | [[Category: Torpedo californica]] | ||
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[[Category: synapse]] | [[Category: synapse]] | ||
- | ''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 13:46:01 2007'' |
Revision as of 11:41, 30 October 2007
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TORPEDO ACETYLCHOLINESTERASE- HG HEAVY-ATOM DERIVATIVE
Overview
Chemical modification of Torpedo californica acetylcholinesterase by, various sulfhydryl reagents results in its conversion to one of two, principal states. One of these states, viz., that produced by disulfides, and alkylating agents, is stable. The second state, produced by mercury, derivatives, is metastable. At room temperature, it converts, spontaneously, with a half-life of ca. 1 h, to a stable state similar to, that produced by the disulfides and alkylating agents. Demodification of, acetylcholinesterase freshly modified by mercurials, by its exposure to, reduced glutathione, causes rapid release of the bound mercurial, with, concomitant recovery of most of the enzymic activity of the native enzyme., In contrast, similar demodification of acetylcholinesterase modified by, ... [(full description)]
About this Structure
2J4F is a [Single protein] structure of sequence from [Torpedo californica] with HG as [ligand]. Active as [Acetylcholinesterase], with EC number [3.1.1.7]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
A metastable state of Torpedo californica acetylcholinesterase generated by modification with organomercurials., Kreimer DI, Dolginova EA, Raves M, Sussman JL, Silman I, Weiner L, Biochemistry. 1994 Dec 6;33(48):14407-18. PMID:7981200
Page seeded by OCA on Tue Oct 30 13:46:01 2007
Categories: Acetylcholinesterase | Single protein | Torpedo californica | Dolginova, E.A. | Kreimer, D.I. | Raves, M. | Silman, I. | Sussman, J.L. | Weiner, L. | HG | Alpha-beta hydrolase | Alternative splicing | Catalytic triad | Cholinesterase | Glycoprotein | Gpi-anchor | Hydrolase | Lipoprotein | Membrane | Neurotransmitter cleavage | Neurotransmitter degradation | Serine esterase | Serine hydrolase | Synapse