2c58

From Proteopedia

(Difference between revisions)

Revision as of 11:55, 10 May 2019

Torpedo californica acetylcholinesterase in complex with 20mM acetylthiocholine

Structural highlights

2c58 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:	, , , ,
NonStd Res:
Related:	1acj, 1acl, 1amn, 1ax9, 1cfj, 1dx6, 1e3q, 1e66, 1ea5, 1eea, 1eve, 1fss, 1gpk, 1gpn, 1gqr, 1gqs, 1h22, 1h23, 1hbj, 1jga, 1jgb, 1jjb, 1oce, 1odc, 1qid, 1qie, 1qif, 1qig, 1qih, 1qii, 1qij, 1qik, 1qim, 1qti, 1som, 1u65, 1ut6, 1vot, 1vxo, 1vxr, 1w4l, 1w6r, 1w75, 1w76, 1zgb, 1zgc, 2ace, 2ack, 2c4h, 2c5f, 2c5g, 2dfp, 3ace, 4ace
Activity:	Acetylcholinesterase, with EC number 3.1.1.7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Acetylcholinesterase (AChE) terminates nerve-impulse transmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter, acetylcholine. Substrate traffic in AChE involves at least two binding sites, the catalytic and peripheral anionic sites, which have been suggested to be allosterically related and involved in substrate inhibition. Here, we present the crystal structures of Torpedo californica AChE complexed with the substrate acetylthiocholine, the product thiocholine and a nonhydrolysable substrate analogue. These structures provide a series of static snapshots of the substrate en route to the active site and identify, for the first time, binding of substrate and product at both the peripheral and active sites. Furthermore, they provide structural insight into substrate inhibition in AChE at two different substrate concentrations. Our structural data indicate that substrate inhibition at moderate substrate concentration is due to choline exit being hindered by a substrate molecule bound at the peripheral site. At the higher concentration, substrate inhibition arises from prevention of exit of acetate due to binding of two substrate molecules within the active-site gorge.

Structural insights into substrate traffic and inhibition in acetylcholinesterase.,Colletier JP, Fournier D, Greenblatt HM, Stojan J, Sussman JL, Zaccai G, Silman I, Weik M EMBO J. 2006 Jun 21;25(12):2746-56. Epub 2006 Jun 8. PMID:16763558^[1]

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

References

↑ Colletier JP, Fournier D, Greenblatt HM, Stojan J, Sussman JL, Zaccai G, Silman I, Weik M. Structural insights into substrate traffic and inhibition in acetylcholinesterase. EMBO J. 2006 Jun 21;25(12):2746-56. Epub 2006 Jun 8. PMID:16763558

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/2c58"

@@ Line 1: / Line 1: @@
-==TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH 20MM ACETYLTHIOCHOLINE==
-<StructureSection load='2c58' size='340' side='right' caption='[[2c58]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+==Torpedo californica acetylcholinesterase in complex with 20mM acetylthiocholine==
+<StructureSection load='2c58' size='340' side='right'caption='[[2c58]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2c58]] is a 1 chain structure with 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=2C58 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C58 FirstGlance]. <br>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1acj|1acj]], [[1acl|1acl]], [[1amn|1amn]], [[1ax9|1ax9]], [[1cfj|1cfj]], [[1dx6|1dx6]], [[1e3q|1e3q]], [[1e66|1e66]], [[1ea5|1ea5]], [[1eea|1eea]], [[1eve|1eve]], [[1fss|1fss]], [[1gpk|1gpk]], [[1gpn|1gpn]], [[1gqr|1gqr]], [[1gqs|1gqs]], [[1h22|1h22]], [[1h23|1h23]], [[1hbj|1hbj]], [[1jga|1jga]], [[1jgb|1jgb]], [[1jjb|1jjb]], [[1oce|1oce]], [[1odc|1odc]], [[1qid|1qid]], [[1qie|1qie]], [[1qif|1qif]], [[1qig|1qig]], [[1qih|1qih]], [[1qii|1qii]], [[1qij|1qij]], [[1qik|1qik]], [[1qim|1qim]], [[1qti|1qti]], [[1som|1som]], [[1u65|1u65]], [[1ut6|1ut6]], [[1vot|1vot]], [[1vxo|1vxo]], [[1vxr|1vxr]], [[1w4l|1w4l]], [[1w6r|1w6r]], [[1w75|1w75]], [[1w76|1w76]], [[1zgb|1zgb]], [[1zgc|1zgc]], [[2ace|2ace]], [[2ack|2ack]], [[2c4h|2c4h]], [[2c5f|2c5f]], [[2c5g|2c5g]], [[2dfp|2dfp]], [[3ace|3ace]], [[4ace|4ace]]</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=2c58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c58 OCA], [http://pdbe.org/2c58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c58 RCSB], [http://www.ebi.ac.uk/pdbsum/2c58 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=2c58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c58 OCA], [http://pdbe.org/2c58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c58 RCSB], [http://www.ebi.ac.uk/pdbsum/2c58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c58 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c5/2c58_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c5/2c58_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 32: / Line 33: @@
 ==See Also==
-*[[3D structures of acetylcholinesterase|3D structures of acetylcholinesterase]]
+*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
 == References ==
 <references/>
@@ Line 38: / Line 39: @@
 </StructureSection>
 [[Category: Acetylcholinesterase]]
+[[Category: Large Structures]]
 [[Category: Torpedo californica]]
 [[Category: Colletier, J P]]
@@ Line 47: / Line 49: @@
 [[Category: Zaccai, G]]
 [[Category: Alpha/beta hydrolase]]
+[[Category: Alternative splicing]]
 [[Category: Glycoprotein]]
 [[Category: Gpi-anchor]]

2c58

From Proteopedia

Revision as of 11:55, 10 May 2019

Torpedo californica acetylcholinesterase in complex with 20mM acetylthiocholine

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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