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| | <StructureSection load='5j6q' size='340' side='right'caption='[[5j6q]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5j6q' size='340' side='right'caption='[[5j6q]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5j6q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clod6 Clod6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J6Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5J6Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5j6q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile_630 Clostridioides difficile 630]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J6Q FirstGlance]. <br> |
| - | </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=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cwp8, CD630_27990 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272563 CLOD6])</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=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5j6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j6q OCA], [http://pdbe.org/5j6q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j6q RCSB], [http://www.ebi.ac.uk/pdbsum/5j6q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j6q ProSAT]</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=5j6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j6q OCA], [https://pdbe.org/5j6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j6q RCSB], [https://www.ebi.ac.uk/pdbsum/5j6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j6q ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q183N4_CLOD6 Q183N4_CLOD6] |
| | <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: Clod6]] | + | [[Category: Clostridioides difficile 630]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Renko, M]] | + | [[Category: Renko M]] |
| - | [[Category: Turk, D]] | + | [[Category: Turk D]] |
| - | [[Category: Usenik, A]] | + | [[Category: Usenik A]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Cell wall protein]]
| + | |
| - | [[Category: Cwb2 domain]]
| + | |
| - | [[Category: S-layer]]
| + | |
| - | [[Category: Toprim fold]]
| + | |
| Structural highlights
Function
Q183N4_CLOD6
Publication Abstract from PubMed
Bacterial cell wall proteins play crucial roles in cell survival, growth, and environmental interactions. In Gram-positive bacteria, cell wall proteins include several types that are non-covalently attached via cell wall binding domains. Of the two conserved surface-layer (S-layer)-anchoring modules composed of three tandem SLH or CWB2 domains, the latter have so far eluded structural insight. The crystal structures of Cwp8 and Cwp6 reveal multi-domain proteins, each containing an embedded CWB2 module. It consists of a triangular trimer of Rossmann-fold CWB2 domains, a feature common to 29 cell wall proteins in Clostridium difficile 630. The structural basis of the intact module fold necessary for its binding to the cell wall is revealed. A comparison with previously reported atomic force microscopy data of S-layers suggests that C. difficile S-layers are complex oligomeric structures, likely composed of several different proteins.
The CWB2 Cell Wall-Anchoring Module Is Revealed by the Crystal Structures of the Clostridium difficile Cell Wall Proteins Cwp8 and Cwp6.,Usenik A, Renko M, Mihelic M, Lindic N, Borisek J, Perdih A, Pretnar G, Muller U, Turk D Structure. 2017 Mar 7;25(3):514-521. doi: 10.1016/j.str.2016.12.018. Epub 2017, Jan 26. PMID:28132783[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Usenik A, Renko M, Mihelic M, Lindic N, Borisek J, Perdih A, Pretnar G, Muller U, Turk D. The CWB2 Cell Wall-Anchoring Module Is Revealed by the Crystal Structures of the Clostridium difficile Cell Wall Proteins Cwp8 and Cwp6. Structure. 2017 Mar 7;25(3):514-521. doi: 10.1016/j.str.2016.12.018. Epub 2017, Jan 26. PMID:28132783 doi:http://dx.doi.org/10.1016/j.str.2016.12.018
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