View source for 5njl


==Cwp2 from Clostridium difficile==
<StructureSection load='5njl' size='340' side='right'caption='[[5njl]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5njl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile_R20291 Clostridioides difficile R20291]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NJL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5njl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5njl OCA], [https://pdbe.org/5njl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5njl RCSB], [https://www.ebi.ac.uk/pdbsum/5njl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5njl ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Colonization of the gut by Clostridium difficile requires the adhesion of the bacterium to host cells. A range of cell surface located factors have been linked to adhesion including the S-layer protein LMW SLP and the related protein Cwp66. As well as these proteins, the S-layer of C. difficile may contain many others. One such protein is Cwp2. Here, we demonstrate the production of a C. difficile strain 630 cwp2 knockout mutant and assess the effect on the bacterium. The mutant results in increased TcdA (toxin A) release and impaired cellular adherence in vitro. We also present the extended three domain structure of the 'functional' region of Cwp2, consisting of residues 29-318 at 1.9 A, which is compared to that of LMW SLP and Cwp8. The adhesive properties of Cwp2 and LMW SLP, which are likely to be shared by Cwp8, are predicted to be mediated by the variable loop regions in domain 2. DATABASES: Structural data are available in the PDB under the accession number 5NJL.

Cwp2 from Clostridium difficile exhibits an extended three domain fold and cell adhesion in vitro.,Bradshaw WJ, Kirby JM, Roberts AK, Shone CC, Acharya KR FEBS J. 2017 Sep;284(17):2886-2898. doi: 10.1111/febs.14157. Epub 2017 Jul 23. PMID:28677344<ref>PMID:28677344</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5njl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Clostridioides difficile R20291]]
[[Category: Large Structures]]
[[Category: Acharya KR]]
[[Category: Bradshaw WJ]]
[[Category: Kirby JM]]
[[Category: Roberts AK]]
[[Category: Shone CC]]