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| | <StructureSection load='4d59' size='340' side='right'caption='[[4d59]], [[Resolution|resolution]] 1.84Å' scene=''> | | <StructureSection load='4d59' size='340' side='right'caption='[[4d59]], [[Resolution|resolution]] 1.84Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d59]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridioides_difficile_qcd-32g58 Clostridioides difficile qcd-32g58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D59 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile_QCD-32g58 Clostridioides difficile QCD-32g58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D59 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=JEF:O-(O-(2-AMINOPROPYL)-O-(2-METHOXYETHYL)POLYPROPYLENE+GLYCOL+500)'>JEF</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=JEF:O-(O-(2-AMINOPROPYL)-O-(2-METHOXYETHYL)POLYPROPYLENE+GLYCOL+500)'>JEF</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d5a|4d5a]]</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=4d59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d59 OCA], [https://pdbe.org/4d59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d59 RCSB], [https://www.ebi.ac.uk/pdbsum/4d59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d59 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_L Cathepsin L], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.15 3.4.22.15] </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=4d59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d59 OCA], [http://pdbe.org/4d59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d59 RCSB], [http://www.ebi.ac.uk/pdbsum/4d59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d59 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cathepsin L]]
| + | [[Category: Clostridioides difficile QCD-32g58]] |
| - | [[Category: Clostridioides difficile qcd-32g58]] | + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Acharya, K R]] | + | [[Category: Acharya KR]] |
| - | [[Category: Bradshaw, W J]] | + | [[Category: Bradshaw WJ]] |
| - | [[Category: Roberts, A K]] | + | [[Category: Roberts AK]] |
| - | [[Category: Shone, C C]] | + | [[Category: Shone CC]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: S-layer]]
| + | |
| - | [[Category: Surface layer]]
| + | |
| Structural highlights
Publication Abstract from PubMed
In recent decades, the global healthcare problems caused by Clostridium difficile have increased at an alarming rate. A greater understanding of this antibiotic-resistant bacterium, particularly with respect to how it interacts with the host, is required for the development of novel strategies for fighting C. difficile infections. The surface layer (S-layer) of C. difficile is likely to be of significant importance to host-pathogen interactions. The mature S-layer is formed by a proteinaceous array consisting of multiple copies of a high-molecular-weight and a low-molecular-weight S-layer protein. These components result from the cleavage of SlpA by Cwp84, a cysteine protease. The structure of a truncated Cwp84 active-site mutant has recently been reported and the key features have been identified, providing the first structural insights into the role of Cwp84 in the formation of the S-layer. Here, two structures of Cwp84 after propeptide cleavage are presented and the three conformational changes that are observed are discussed. These changes result in a reconfiguration of the active site and exposure of the hydrophobic pocket.
Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide.,Bradshaw WJ, Roberts AK, Shone CC, Acharya KR Acta Crystallogr F Struct Biol Commun. 2015 Mar 1;71(Pt 3):295-303. doi:, 10.1107/S2053230X15001065. Epub 2015 Feb 19. PMID:25760704[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bradshaw WJ, Roberts AK, Shone CC, Acharya KR. Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide. Acta Crystallogr F Struct Biol Commun. 2015 Mar 1;71(Pt 3):295-303. doi:, 10.1107/S2053230X15001065. Epub 2015 Feb 19. PMID:25760704 doi:http://dx.doi.org/10.1107/S2053230X15001065
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