6tsb: Difference between revisions

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-'''Unreleased structure'''
-The entry 6tsb is ON HOLD
+==Crystal structure of the Chitinase Domain of the Spore Coat Protein CotE from Clostridium difficile==
+<StructureSection load='6tsb' size='340' side='right'caption='[[6tsb]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TSB 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]] 2.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=6tsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tsb OCA], [https://pdbe.org/6tsb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tsb RCSB], [https://www.ebi.ac.uk/pdbsum/6tsb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tsb ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+CotE is a coat protein that is present in the spores of Clostridium difficile, an obligate anaerobic bacterium and a pathogen that is a leading cause of antibiotic-associated diarrhoea in hospital patients. Spores serve as the agents of disease transmission, and CotE has been implicated in their attachment to the gut epithelium and subsequent colonization of the host. CotE consists of an N-terminal peroxiredoxin domain and a C-terminal chitinase domain. Here, a C-terminal fragment of CotE comprising residues 349-712 has been crystallized and its structure has been determined to reveal a core eight-stranded beta-barrel fold with a neighbouring subdomain containing a five-stranded beta-sheet. A prominent groove running across the top of the barrel is lined by residues that are conserved in family 18 glycosyl hydrolases and which participate in catalysis. Electron density identified in the groove defines the pentapeptide Gly-Pro-Ala-Met-Lys derived from the N-terminus of the protein following proteolytic cleavage to remove an affinity-purification tag. These observations suggest the possibility of designing peptidomimetics to block C. difficile transmission.
-Authors:
+Crystal structures of the GH18 domain of the bifunctional peroxiredoxin-chitinase CotE from Clostridium difficile.,Whittingham JL, Hanai S, Brannigan JA, Ferreira WT, Dodson EJ, Turkenburg JP, Cartwright J, Cutting SM, Wilkinson AJ Acta Crystallogr F Struct Biol Commun. 2020 Jun 1;76(Pt 6):241-249. doi:, 10.1107/S2053230X20006147. Epub 2020 May 29. PMID:32510464<ref>PMID:32510464</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6tsb" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Dodson EJ]]
+[[Category: Whittingham JL]]
+[[Category: Wilkinson AJ]]