6oks: Difference between revisions

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<SX load='6oks' size='340' side='right' viewer='molstar' caption='[[6oks]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
<SX load='6oks' size='340' side='right' viewer='molstar' caption='[[6oks]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6oks]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OKS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OKS FirstGlance]. <br>
<table><tr><td colspan='2'>[[6oks]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile Clostridioides difficile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OKS FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cdtB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 "Bacillus difficilis" Hall and O'Toole 1935])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6oks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oks OCA], [http://pdbe.org/6oks PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oks RCSB], [http://www.ebi.ac.uk/pdbsum/6oks PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oks 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=6oks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oks OCA], [https://pdbe.org/6oks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oks RCSB], [https://www.ebi.ac.uk/pdbsum/6oks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oks ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A8DS70_CLODI A8DS70_CLODI]
Clostridioides (formerly Clostridium) difficile is a Gram-positive, spore-forming anaerobe and a leading cause of hospital-acquired infection and gastroenteritis-associated death in US hospitals(1). The disease state is usually preceded by disruption of the host microbiome in response to antibiotic treatment and is characterized by mild to severe diarrhoea. C. difficile infection is dependent on the secretion of one or more AB-type toxins: toxin A (TcdA), toxin B (TcdB) and the C. difficile transferase toxin (CDT)(2). Whereas TcdA and TcdB are considered the primary virulence factors, recent studies suggest that CDT increases the severity of C. difficile infection in some of the most problematic clinical strains(3). To better understand how CDT functions, we used cryo-electron microscopy to define the structure of CDTb, the cell-binding component of CDT. We obtained structures of several oligomeric forms that highlight the conformational changes that enable conversion from a prepore to a beta-barrel pore. The structural analysis also reveals a glycan-binding domain and residues involved in binding the host-cell receptor, lipolysis-stimulated lipoprotein receptor. Together, these results provide a framework to understand how CDT functions at the host cell interface.
 
Structural insights into the transition of Clostridioides difficile binary toxin from prepore to pore.,Anderson DM, Sheedlo MJ, Jensen JL, Lacy DB Nat Microbiol. 2020 Jan;5(1):102-107. doi: 10.1038/s41564-019-0601-8. Epub 2019, Nov 11. PMID:31712627<ref>PMID:31712627</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6oks" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
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[[Category: Bacillus difficilis hall and o'toole 1935]]
[[Category: Clostridioides difficile]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Anderson, D M]]
[[Category: Anderson DM]]
[[Category: Lacy, D B]]
[[Category: Lacy DB]]
[[Category: Sheedlo, M J]]
[[Category: Sheedlo MJ]]
[[Category: Binary]]
[[Category: Cdtb]]
[[Category: Clostridium]]
[[Category: Difficil]]
[[Category: Toxin]]
[[Category: Transferase]]

Latest revision as of 12:24, 20 March 2024

CDTb Double Heptamer Long Form Mask 1 Modeled from Cryo-EM Map Reconstructed using C7 SymmetryCDTb Double Heptamer Long Form Mask 1 Modeled from Cryo-EM Map Reconstructed using C7 Symmetry

6oks, resolution 4.20Å

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