1fas: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 3: Line 3:
<StructureSection load='1fas' size='340' side='right'caption='[[1fas]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1fas' size='340' side='right'caption='[[1fas]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fas]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bmnh_1946.1.20.48 Bmnh 1946.1.20.48]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FAS FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fas]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FAS FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fas OCA], [https://pdbe.org/1fas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fas RCSB], [https://www.ebi.ac.uk/pdbsum/1fas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fas ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fas OCA], [https://pdbe.org/1fas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fas RCSB], [https://www.ebi.ac.uk/pdbsum/1fas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fas ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/3SE1_DENAN 3SE1_DENAN] Interferes with neuromuscular transmission by inhibiting the enzyme acetylcholinesterase (AChE) present at the neuromuscular junction. It selectively binds and inhibits with a 1:1 stoichiometry the mammalian and electric fish AChE at picomolar concentrations. It is highly specific for the peripheral site of AChE and blocks the entry of acetylcholine into the active site of the enzyme, thereby preventing its breakdown. It has been called fasciculin since after injection into mice it causes severe, generalized and long-lasting (5-7 hours) fasciculations.<ref>PMID:6530667</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 16: Line 19:
</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=1fas 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=1fas ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of fasciculin 1, a potent acetylcholinesterase inhibitor from green mamba snake venom, has been solved by the multiple isomorphous replacement method complemented with anomalous scattering and subsequently refined at 1.9-A resolution. The overall structure of fasciculin is similar to those of the short alpha-neurotoxins and cardiotoxins, with a dense core rich in disulfide bridges and three long loops disposed as the central fingers of a hand. A comparison of these three prototypic toxin types shows that fasciculin 1 has structural features that are intermediate between those of the other two molecules. Its core region, which can be defined as a continuous stretch of conserved residues, is very similar to that of erabutoxin b, whereas the orientation of its long loops resembles that of cardiotoxin VII4. This result introduces a new element in the study of phylogenetic relationships of snake toxins and suggests that, after divergency from an ancestral gene, convergent evolution may have played an important factor in the evolution of these proteins. In fasciculin 1, several arginine and lysine residues are well ordered and relatively exposed to the solvent medium and may play a role in the binding to the peripheral site of acetylcholinesterases.
1.9-A resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom.,le Du MH, Marchot P, Bougis PE, Fontecilla-Camps JC J Biol Chem. 1992 Nov 5;267(31):22122-30. PMID:1429564<ref>PMID:1429564</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fas" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
Line 32: Line 26:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bmnh 1946 1.20 48]]
[[Category: Dendroaspis angusticeps]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bougis, P E]]
[[Category: Bougis PE]]
[[Category: Du, M H.Le]]
[[Category: Fontecilla-Camps JC]]
[[Category: Fontecilla-Camps, J C]]
[[Category: Le Du MH]]
[[Category: Marchot, P]]
[[Category: Marchot P]]
[[Category: Toxin]]

Revision as of 13:12, 20 March 2024

1.9 ANGSTROM RESOLUTION STRUCTURE OF FASCICULIN 1, AN ANTI-ACETYLCHOLINESTERASE TOXIN FROM GREEN MAMBA SNAKE VENOM1.9 ANGSTROM RESOLUTION STRUCTURE OF FASCICULIN 1, AN ANTI-ACETYLCHOLINESTERASE TOXIN FROM GREEN MAMBA SNAKE VENOM

Structural highlights

1fas is a 1 chain structure with sequence from Dendroaspis angusticeps. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

3SE1_DENAN Interferes with neuromuscular transmission by inhibiting the enzyme acetylcholinesterase (AChE) present at the neuromuscular junction. It selectively binds and inhibits with a 1:1 stoichiometry the mammalian and electric fish AChE at picomolar concentrations. It is highly specific for the peripheral site of AChE and blocks the entry of acetylcholine into the active site of the enzyme, thereby preventing its breakdown. It has been called fasciculin since after injection into mice it causes severe, generalized and long-lasting (5-7 hours) fasciculations.[1]

Evolutionary Conservation

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

See Also

References

  1. ↑ Karlsson E, Mbugua PM, Rodriguez-Ithurralde D. Fasciculins, anticholinesterase toxins from the venom of the green mamba Dendroaspis angusticeps. J Physiol (Paris). 1984;79(4):232-40. PMID:6530667

1fas, resolution 1.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1fas&oldid=4108874"