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2wg1

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Revision as of 19:05, 8 February 2016

TERNARY COMPLEX OF THE AGED CONJUGATE OF TORPEDO CALIFORNICA ACEYLCHOLINESTERASE WITH SOMAN AND 2-PAM

Structural highlights

2wg1 is a 1 chain structure with sequence from Torpedo californica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , ,
Related:	1zgb, 1qti, 1amn, 1e66, 2vq6, 2ack, 2j3d, 1qii, 2ckm, 1dx6, 1qij, 1qie, 1acl, 1w4l, 1odc, 2cmf, 2wg0, 1gqs, 2j3q, 1e3q, 2j4f, 1qik, 2dfp, 2c5f, 1ea5, 1eea, 1qif, 2vjc, 2vjb, 1qig, 1zgc, 1qid, 2wfz, 2vjd, 1jjb, 1ut6, 2vt6, 2w9i, 2wg2, 2vt7, 2cek, 1qim, 1gpk, 1jga, 3ace, 1oce, 1w6r, 1som, 1vxo, 2vja, 2w6c, 1cfj, 2v96, 1ax9, 1u65, 1w76, 1h22, 1eve, 2c4h, 1gqr, 2ace, 2va9, 1vxr, 4ace, 2c58, 1hbj, 1vot, 1w75, 2c5g, 2v98, 1jgb, 1gpn, 1qih, 1h23, 1acj, 1fss, 2v97
Activity:	Acetylcholinesterase, with EC number 3.1.1.7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[ACES_TORCA] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Organophosphate compounds (OP) are potent inhibitors of acetylcholinesterases (AChEs) and can cause lethal poisoning in humans. Inhibition of AChEs by the OP soman involves phosphonylation of the catalytic serine, and subsequent dealkylation produces a form known as the "aged" enzyme. The nonaged form can be reactivated to a certain extent by nucleophiles, such as pralidoxime (2-PAM), whereas aged forms of OP-inhibited AChEs are totally resistant to reactivation. Here, we solved the X-ray crystal structures of AChE from Torpedo californica (TcAChE) conjugated with soman before and after aging. The absolute configuration of the soman stereoisomer adduct in the nonaged conjugate is P(S)C(R). A structural reorientation of the catalytic His440 side chain was observed during the aging process. Furthermore, the crystal structure of the ternary complex of the aged conjugate with 2-PAM revealed that the orientation of the oxime function does not permit nucleophilic attack on the phosphorus atom, thus providing a plausible explanation for its failure to reactivate the aged soman/AChE conjugate. Together, these three crystal structures provide an experimental basis for the design of new reactivators.

Crystallographic Snapshots of Nonaged and Aged Conjugates of Soman with Acetylcholinesterase, and of a Ternary Complex of the Aged Conjugate with Pralidoxime (dagger).,Sanson B, Nachon F, Colletier JP, Froment MT, Toker L, Greenblatt HM, Sussman JL, Ashani Y, Masson P, Silman I, Weik M J Med Chem. 2009 Jul 30. PMID:19642642^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sanson B, Nachon F, Colletier JP, Froment MT, Toker L, Greenblatt HM, Sussman JL, Ashani Y, Masson P, Silman I, Weik M. Crystallographic Snapshots of Nonaged and Aged Conjugates of Soman with Acetylcholinesterase, and of a Ternary Complex of the Aged Conjugate with Pralidoxime (dagger). J Med Chem. 2009 Jul 30. PMID:19642642 doi:10.1021/jm900433t

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wg1"

@@ Line 6: / Line 6: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zgb|1zgb]], [[1qti|1qti]], [[1amn|1amn]], [[1e66|1e66]], [[2vq6|2vq6]], [[2ack|2ack]], [[2j3d|2j3d]], [[1qii|1qii]], [[2ckm|2ckm]], [[1dx6|1dx6]], [[1qij|1qij]], [[1qie|1qie]], [[1acl|1acl]], [[1w4l|1w4l]], [[1odc|1odc]], [[2cmf|2cmf]], [[2wg0|2wg0]], [[1gqs|1gqs]], [[2j3q|2j3q]], [[1e3q|1e3q]], [[2j4f|2j4f]], [[1qik|1qik]], [[2dfp|2dfp]], [[2c5f|2c5f]], [[1ea5|1ea5]], [[1eea|1eea]], [[1qif|1qif]], [[2vjc|2vjc]], [[2vjb|2vjb]], [[1qig|1qig]], [[1zgc|1zgc]], [[1qid|1qid]], [[2wfz|2wfz]], [[2vjd|2vjd]], [[1jjb|1jjb]], [[1ut6|1ut6]], [[2vt6|2vt6]], [[2w9i|2w9i]], [[2wg2|2wg2]], [[2vt7|2vt7]], [[2cek|2cek]], [[1qim|1qim]], [[1gpk|1gpk]], [[1jga|1jga]], [[3ace|3ace]], [[1oce|1oce]], [[1w6r|1w6r]], [[1som|1som]], [[1vxo|1vxo]], [[2vja|2vja]], [[2w6c|2w6c]], [[1cfj|1cfj]], [[2v96|2v96]], [[1ax9|1ax9]], [[1u65|1u65]], [[1w76|1w76]], [[1h22|1h22]], [[1eve|1eve]], [[2c4h|2c4h]], [[1gqr|1gqr]], [[2ace|2ace]], [[2va9|2va9]], [[1vxr|1vxr]], [[4ace|4ace]], [[2c58|2c58]], [[1hbj|1hbj]], [[1vot|1vot]], [[1w75|1w75]], [[2c5g|2c5g]], [[2v98|2v98]], [[1jgb|1jgb]], [[1gpn|1gpn]], [[1qih|1qih]], [[1h23|1h23]], [[1acj|1acj]], [[1fss|1fss]], [[2v97|2v97]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wg1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wg1 RCSB], [http://www.ebi.ac.uk/pdbsum/2wg1 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wg1 OCA], [http://pdbe.org/2wg1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wg1 RCSB], [http://www.ebi.ac.uk/pdbsum/2wg1 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 18: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2wg1 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2wg1" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 35: / Line 36: @@
 *[[Acetylcholinesterase inhibitors|Acetylcholinesterase inhibitors]]
 *[[Acetylcholinesterase with DFP|Acetylcholinesterase with DFP]]
+*[[3D structures of acetylcholinesterase|3D structures of acetylcholinesterase]]
 == References ==
 <references/>

2wg1

From Proteopedia

Revision as of 19:05, 8 February 2016

TERNARY COMPLEX OF THE AGED CONJUGATE OF TORPEDO CALIFORNICA ACEYLCHOLINESTERASE WITH SOMAN AND 2-PAM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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