1s3r: Difference between revisions

Revision as of 15:57, 21 February 2008

Crystal structure of the human-specific toxin intermedilysin

OverviewOverview

The cholesterol-dependent cytolysins (CDCs), a superfamily of pore-forming toxins, are characterized by a conserved undecapeptide motif that is believed to be critical for membrane recognition by means of cholesterol. Intermedilysin (ILY), an unusual member of the CDCs, exhibits specificity for human cells and contains nonconservative substitutions in the motif. We show that the cellular specificity of ILY is based on its ability to specifically bind to human cells and does not involve some other feature of the CDC mechanism. Furthermore, cellular recognition by ILY appears to be encoded in domain 4 alone but does not involve the variant undecapeptide of ILY. We show that the undecapeptide is involved in the prepore-to-pore conversion of ILY and so demonstrate a direct connection between the structure of the undecapeptide and the prepore-to-pore transition. We have determined the crystal structure of ILY, which, when compared to the known structure of a prototypical CDC, suggests that the basic aspects of its 3D structure are likely to be conserved in all CDCs.

About this StructureAbout this Structure

1S3R is a Single protein structure of sequence from Streptococcus intermedius with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin., Polekhina G, Giddings KS, Tweten RK, Parker MW, Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):600-5. Epub 2005 Jan 6. PMID:15637162

Page seeded by OCA on Thu Feb 21 14:57:40 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1s3r.gif|left|200px]]<br /><applet load="1s3r" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1s3r.gif|left|200px]]<br /><applet load="1s3r" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1s3r, resolution 2.60&Aring;" />
 '''Crystal structure of the human-specific toxin intermedilysin'''<br />
 ==Overview==
-The cholesterol-dependent cytolysins (CDCs), a superfamily of pore-forming, toxins, are characterized by a conserved undecapeptide motif that is, believed to be critical for membrane recognition by means of cholesterol., Intermedilysin (ILY), an unusual member of the CDCs, exhibits specificity, for human cells and contains nonconservative substitutions in the motif., We show that the cellular specificity of ILY is based on its ability to, specifically bind to human cells and does not involve some other feature, of the CDC mechanism. Furthermore, cellular recognition by ILY appears to, be encoded in domain 4 alone but does not involve the variant, undecapeptide of ILY. We show that the undecapeptide is involved in the, prepore-to-pore conversion of ILY and so demonstrate a direct connection, between the structure of the undecapeptide and the prepore-to-pore, transition. We have determined the crystal structure of ILY, which, when, compared to the known structure of a prototypical CDC, suggests that the, basic aspects of its 3D structure are likely to be conserved in all CDCs.
+The cholesterol-dependent cytolysins (CDCs), a superfamily of pore-forming toxins, are characterized by a conserved undecapeptide motif that is believed to be critical for membrane recognition by means of cholesterol. Intermedilysin (ILY), an unusual member of the CDCs, exhibits specificity for human cells and contains nonconservative substitutions in the motif. We show that the cellular specificity of ILY is based on its ability to specifically bind to human cells and does not involve some other feature of the CDC mechanism. Furthermore, cellular recognition by ILY appears to be encoded in domain 4 alone but does not involve the variant undecapeptide of ILY. We show that the undecapeptide is involved in the prepore-to-pore conversion of ILY and so demonstrate a direct connection between the structure of the undecapeptide and the prepore-to-pore transition. We have determined the crystal structure of ILY, which, when compared to the known structure of a prototypical CDC, suggests that the basic aspects of its 3D structure are likely to be conserved in all CDCs.
 ==About this Structure==
-S3R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_intermedius Streptococcus intermedius] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S3R OCA].
+S3R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_intermedius Streptococcus intermedius] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S3R OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Streptococcus intermedius]]
-[[Category: Giddings, K.S.]]
+[[Category: Giddings, K S.]]
-[[Category: Parker, M.W.]]
+[[Category: Parker, M W.]]
 [[Category: Polekhina, G.]]
-[[Category: Tweten, R.K.]]
+[[Category: Tweten, R K.]]
 [[Category: SO4]]
 [[Category: toxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:51:06 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:40 2008''