1sr4
From Proteopedia
(Difference between revisions)
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<StructureSection load='1sr4' size='340' side='right'caption='[[1sr4]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1sr4' size='340' side='right'caption='[[1sr4]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1sr4]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1sr4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_ducreyi Haemophilus ducreyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SR4 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sr4 OCA], [https://pdbe.org/1sr4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sr4 RCSB], [https://www.ebi.ac.uk/pdbsum/1sr4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sr4 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/CDTA_HAEDU CDTA_HAEDU] CDTs are cytotoxins which induce host cell distension, growth arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in HeLa cells. CdtA, along with CdtC, probably forms a heterodimeric subunit required for the delivery of CdtB. |
== 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=1sr4 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=1sr4 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The tripartite cytolethal distending toxin (CDT) induces cell cycle arrest and apoptosis in eukaryotic cells. The subunits CdtA and CdtC associate with the nuclease CdtB to form a holotoxin that translocates CdtB into the host cell, where it acts as a genotoxin by creating DNA lesions. Here we show that the crystal structure of the holotoxin from Haemophilus ducreyi reveals that CDT consists of an enzyme of the DNase-I family, bound to two ricin-like lectin domains. CdtA, CdtB and CdtC form a ternary complex with three interdependent molecular interfaces, characterized by globular, as well as extensive non-globular, interactions. The lectin subunits form a deeply grooved, highly aromatic surface that we show to be critical for toxicity. The holotoxin possesses a steric block of the CdtB active site by means of a non-globular extension of the CdtC subunit, and we identify putative DNA binding residues in CdtB that are essential for toxin activity. | ||
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- | Assembly and function of a bacterial genotoxin.,Nesic D, Hsu Y, Stebbins CE Nature. 2004 May 27;429(6990):429-33. PMID:15164065<ref>PMID:15164065</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1sr4" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Bacillus ulceris cancrosi kruse 1896]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Hsu | + | [[Category: Hsu Y]] |
- | [[Category: Nesic | + | [[Category: Nesic D]] |
- | [[Category: Stebbins | + | [[Category: Stebbins CE]] |
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Revision as of 08:34, 1 May 2024
Crystal Structure of the Haemophilus ducreyi cytolethal distending toxin
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