6t9m: Difference between revisions
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==Crystal structure of the Chitinase Domain of the Spore Coat Protein CotE from Clostridium difficile== | |||
<StructureSection load='6t9m' size='340' side='right'caption='[[6t9m]], [[Resolution|resolution]] 1.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6t9m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile_630 Clostridioides difficile 630] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T9M 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]] 1.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <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=6t9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t9m OCA], [https://pdbe.org/6t9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t9m RCSB], [https://www.ebi.ac.uk/pdbsum/6t9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t9m ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q18BV5_CLOD6 Q18BV5_CLOD6] Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.[HAMAP-Rule:MF_00401] | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6t9m" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Clostridioides difficile 630]] | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Dodson EJ]] | |||
[[Category: Whittingham JL]] | |||
[[Category: Wilkinson AJ]] | |||
Latest revision as of 16:08, 6 November 2024
Crystal structure of the Chitinase Domain of the Spore Coat Protein CotE from Clostridium difficileCrystal structure of the Chitinase Domain of the Spore Coat Protein CotE from Clostridium difficile
Structural highlights
FunctionQ18BV5_CLOD6 Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.[HAMAP-Rule:MF_00401] Publication Abstract from PubMedCotE 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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