2j4f

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[[Image:2j4f.gif|left|200px]]<br /><applet load="2j4f" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2j4f.gif|left|200px]]
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caption="2j4f, resolution 2.8&Aring;" />
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'''TORPEDO ACETYLCHOLINESTERASE- HG HEAVY-ATOM DERIVATIVE'''<br />
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{{Structure
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|PDB= 2j4f |SIZE=350|CAPTION= <scene name='initialview01'>2j4f</scene>, resolution 2.8&Aring;
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|SITE= <scene name='pdbsite=AC1:Hg+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''TORPEDO ACETYLCHOLINESTERASE- HG HEAVY-ATOM DERIVATIVE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=HG:'>HG</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Hg+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J4F OCA].
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2J4F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J4F OCA].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/7981200 7981200]
[[Category: Acetylcholinesterase]]
[[Category: Acetylcholinesterase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: synapse]]
[[Category: synapse]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:59:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:37:03 2008''

Revision as of 15:37, 20 March 2008

Image:2j4f.gif


PDB ID 2j4f

Drag the structure with the mouse to rotate
, resolution 2.8Å
Sites:
Ligands:
Activity: Acetylcholinesterase, with EC number 3.1.1.7
Coordinates: save as pdb, mmCIF, xml



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.

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

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