2j4f: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2j4f.gif|left|200px]]
{{Seed}}
[[Image:2j4f.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2j4f|  PDB=2j4f  |  SCENE=  }}  
{{STRUCTURE_2j4f|  PDB=2j4f  |  SCENE=  }}  


'''TORPEDO ACETYLCHOLINESTERASE- HG HEAVY-ATOM DERIVATIVE'''
===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 disulfides yields no detectable recovery of enzymic activity. Spectroscopic measurements, employing CD, intrinsic fluorescence, and binding of 1-anilino-8-naphthalenesulfonate, show that the state produced initially by mercurials is "native-like", whereas that produced by disulfides and alkylating agents, and after prolonged incubation of the mercurial-modified enzyme, is partially unfolded and displays many of the features of the "molten globule" state. Arrhenius plots show that the quasi-native state produced by organomercurials is separated by a low (5 kcal/mol) energy barrier from the native state, whereas the partially unfolded state is separated from the quasi-native state by a high energy barrier (ca. 50 kcal/mol). Comparison of the 3D structures of native acetylcholinesterase and of a heavy-atom derivative obtained with HgAc2 suggests that the mercurial-modified enzyme may be stabilized by additional interactions of the mercury atom attached to the free thiol group of Cys231, specifically with Ser228O gamma with the main-chain nitrogen and carbonyl oxygen of the same serine residue.
The line below this paragraph, {{ABSTRACT_PUBMED_7981200}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7981200 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_7981200}}


==About this Structure==
==About this Structure==
Line 43: Line 47:
[[Category: Serine hydrolase]]
[[Category: Serine hydrolase]]
[[Category: Synapse]]
[[Category: Synapse]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:18:56 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 6 12:06:53 2008''

Revision as of 09:06, 6 July 2008

File:2j4f.png

Template:STRUCTURE 2j4f

TORPEDO ACETYLCHOLINESTERASE- HG HEAVY-ATOM DERIVATIVE

Template:ABSTRACT PUBMED 7981200

About this Structure

2J4F is a Single protein structure of sequence from Torpedo californica. 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 Sun Jul 6 12:06:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2j4f&oldid=637182"