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| | ==High resolution structure of the functional region of Cwp19 from Clostridium difficile== | | ==High resolution structure of the functional region of Cwp19 from Clostridium difficile== |
| - | <StructureSection load='5oq3' size='340' side='right' caption='[[5oq3]], [[Resolution|resolution]] 1.35Å' scene=''> | + | <StructureSection load='5oq3' size='340' side='right'caption='[[5oq3]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5oq3]] is a 1 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=5OQ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OQ3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5oq3]] is a 1 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=5OQ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OQ3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lytC_21, cwp19, lytC_5, SAMEA3374989_00994, SAMEA3375004_02322 ([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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylmuramoyl-L-alanine_amidase N-acetylmuramoyl-L-alanine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.28 3.5.1.28] </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=5oq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oq3 OCA], [https://pdbe.org/5oq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oq3 RCSB], [https://www.ebi.ac.uk/pdbsum/5oq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oq3 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5oq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oq3 OCA], [http://pdbe.org/5oq3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oq3 RCSB], [http://www.ebi.ac.uk/pdbsum/5oq3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oq3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/L7PGA3_CLODI L7PGA3_CLODI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus difficilis hall and o'toole 1935]] | + | [[Category: Clostridioides difficile]] |
| - | [[Category: N-acetylmuramoyl-L-alanine amidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Acharya, K R]] | + | [[Category: Acharya KR]] |
| - | [[Category: Bradshaw, W J]] | + | [[Category: Bradshaw WJ]] |
| - | [[Category: Kirby, J M]] | + | [[Category: Kirby JM]] |
| - | [[Category: Roberts, A K]] | + | [[Category: Roberts AK]] |
| - | [[Category: Shone, C C]] | + | [[Category: Shone CC]] |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: S-layer]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
L7PGA3_CLODI
Publication Abstract from PubMed
Clostridium difficile is a burden to health care systems around the world, causing tens of thousands of deaths annually. The S-layer of the bacterium, a layer of protein found of the surface of cells, has received a significant amount of attention over the past two decades as a potential target to combat the growing threat presented by C. difficile infections. The S-layer contains a wide range of proteins, each of which possess three cell wall binding domains, while many also possess a "functional" region. Here, we present the high resolution structure of the functional region of one such protein, Cwp19 along with preliminary functional characterisation of the predicted glycoside hydrolase. Cwp19 has a TIM barrel fold and appears to possess a high degree of substrate selectivity. The protein also exhibits peptidoglycan hydrolase activity an order of magnitude slower than that of lysozyme and is the first member of glycoside hydrolase-like family 10 to be characterised. This research goes some way to understanding the role of Cwp19 in the S-layer of C. difficile. This article is protected by copyright. All rights reserved.
The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.,Bradshaw WJ, Kirby JM, Roberts AK, Shone CC, Acharya KR FEBS J. 2017 Oct 30. doi: 10.1111/febs.14310. PMID:29083543[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bradshaw WJ, Kirby JM, Roberts AK, Shone CC, Acharya KR. The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile. FEBS J. 2017 Oct 30. doi: 10.1111/febs.14310. PMID:29083543 doi:http://dx.doi.org/10.1111/febs.14310
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