1fas: Difference between revisions

Revision as of 13:36, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1FAS is a Single protein structure of sequence from Dendroaspis angusticeps. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 12:36:43 2008

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OCA

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-[[Image:1fas.jpg|left|200px]]<br /><applet load="1fas" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fas.jpg|left|200px]]<br /><applet load="1fas" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fas, resolution 1.8&Aring;" />
 '''1.9 ANGSTROM RESOLUTION STRUCTURE OF FASCICULIN 1, AN ANTI-ACETYLCHOLINESTERASE TOXIN FROM GREEN MAMBA SNAKE VENOM'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-FAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FAS OCA].
+FAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://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].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Dendroaspis angusticeps]]
 [[Category: Single protein]]
-[[Category: Bougis, P.E.]]
+[[Category: Bougis, P E.]]
-[[Category: Du, M.H.Le.]]
+[[Category: Du, M H.Le.]]
-[[Category: Fontecilla-Camps, J.C.]]
+[[Category: Fontecilla-Camps, J C.]]
 [[Category: Marchot, P.]]
 [[Category: toxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:46:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:43 2008''