4ci7

<table><tr><td colspan='2'>[[4ci7]] 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=4CI7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CI7 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4ci7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ci7 OCA], [http://pdbe.org/4ci7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ci7 RCSB], [http://www.ebi.ac.uk/pdbsum/4ci7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ci7 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Clostridium difficile is a major problem as an aetiological agent for antibiotic-associated diarrhoea. The mechanism by which the bacterium colonizes the gut during infection is poorly understood, but undoubtedly involves a myriad of components present on the bacterial surface. The mechanism of C. difficile surface-layer (S-layer) biogenesis is also largely unknown but involves the post-translational cleavage of a single polypeptide (surface-layer protein A; SlpA) into low- and high-molecular-weight subunits by Cwp84, a surface-located cysteine protease. Here, the first crystal structure of the surface protein Cwp84 is described at 1.4 A resolution and the key structural components are identified. The truncated Cwp84 active-site mutant (amino-acid residues 33-497; C116A) exhibits three regions: a cleavable propeptide and a cysteine protease domain which exhibits a cathepsin L-like fold followed by a newly identified putative carbohydrate-binding domain with a bound calcium ion, which is referred to here as a lectin-like domain. This study thus provides the first structural insights into Cwp84 and a strong base to elucidate its role in the C. difficile S-layer maturation mechanism.

The structure of the cysteine protease and lectin-like domains of Cwp84, a surface layer-associated protein from Clostridium difficile.,Bradshaw WJ, Kirby JM, Thiyagarajan N, Chambers CJ, Davies AH, Roberts AK, Shone CC, Acharya KR Acta Crystallogr D Biol Crystallogr. 2014 Jul 1;70(Pt 7):1983-93. doi:, 10.1107/S1399004714009997. Epub 2014 Jun 29. PMID:25004975<ref>PMID:25004975</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Clostridioides difficile qcd-32g58]]

[[Category: Acharya, K R]]

[[Category: Bradshaw, W J]]

[[Category: Chambers, C J]]

[[Category: Davies, A H]]

[[Category: Kirby, J M]]

[[Category: Roberts, A K]]

[[Category: Shone, C C]]

[[Category: Thiyagarajan, N]]

[[Category: Surface protein]]