1s3r

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Current revision (13:29, 13 March 2024) (edit) (undo)
 
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<StructureSection load='1s3r' size='340' side='right'caption='[[1s3r]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1s3r' size='340' side='right'caption='[[1s3r]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1s3r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_27335 Atcc 27335]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S3R FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1s3r]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S3R FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1s3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s3r OCA], [https://pdbe.org/1s3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s3r RCSB], [https://www.ebi.ac.uk/pdbsum/1s3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s3r ProSAT]</span></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=1s3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s3r OCA], [https://pdbe.org/1s3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s3r RCSB], [https://www.ebi.ac.uk/pdbsum/1s3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s3r ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9LCB8_STRIT Q9LCB8_STRIT]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1s3r 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=1s3r ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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<ref>PMID:15637162</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1s3r" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Cytolysin 3D structures|Cytolysin 3D structures]]
*[[Cytolysin 3D structures|Cytolysin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 27335]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Giddings, K S]]
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[[Category: Streptococcus intermedius]]
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[[Category: Parker, M W]]
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[[Category: Giddings KS]]
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[[Category: Polekhina, G]]
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[[Category: Parker MW]]
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[[Category: Tweten, R K]]
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[[Category: Polekhina G]]
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[[Category: Toxin]]
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[[Category: Tweten RK]]

Current revision

Crystal structure of the human-specific toxin intermedilysin

PDB ID 1s3r

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