1s3r
From Proteopedia
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- | [[Image:1s3r.gif|left|200px]] | + | [[Image:1s3r.gif|left|200px]] |
- | + | ||
- | '''Crystal structure of the human-specific toxin intermedilysin''' | + | {{Structure |
+ | |PDB= 1s3r |SIZE=350|CAPTION= <scene name='initialview01'>1s3r</scene>, resolution 2.60Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of the human-specific toxin intermedilysin''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1S3R is a [ | + | 1S3R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_intermedius Streptococcus intermedius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S3R OCA]. |
==Reference== | ==Reference== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15637162 15637162] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus intermedius]] | [[Category: Streptococcus intermedius]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:00:01 2008'' |
Revision as of 12:00, 20 March 2008
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, resolution 2.60Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of the human-specific toxin intermedilysin
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.
About this Structure
1S3R is a Single protein structure of sequence from Streptococcus intermedius. Full crystallographic information is available from OCA.
Reference
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
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