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3cvz
From Proteopedia
(Difference between revisions)
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<StructureSection load='3cvz' size='340' side='right'caption='[[3cvz]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3cvz' size='340' side='right'caption='[[3cvz]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3cvz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3cvz]] is a 4 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=3CVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CVZ FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3cvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cvz OCA], [https://pdbe.org/3cvz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cvz RCSB], [https://www.ebi.ac.uk/pdbsum/3cvz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cvz 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=3cvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cvz OCA], [https://pdbe.org/3cvz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cvz RCSB], [https://www.ebi.ac.uk/pdbsum/3cvz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cvz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q183M8_CLOD6 Q183M8_CLOD6] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cvz ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cvz ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Clostridium difficile expresses a surface layer (S-layer) which coats the surface of the bacterium and acts as an adhesin facilitating interaction of the bacterium with host enteric cells. The S-layer contains a high-molecular-weight S-layer protein (HMW SLP) and its low-molecular-weight partner protein (LMW SLP). We show that these proteins form a tightly associated non-covalent complex, the H/L complex, and we identify the regions of both proteins responsible for complex formation. The 2.4 A X-ray crystal structure of a truncated derivative of the LMW SLP reveals two domains. Domain 1 has a two-layer sandwich architecture while domain 2, predicted to orientate towards the external environment, contains a novel fold. Small-angle X-ray scattering analysis of the H/L complex shows an elongated molecule, with the two SLPs arranged 'end-to-end' interacting with each other through a small contact area. Alignment of LMW SLPs, which exhibit high sequence diversity, reveals a core of conserved residues that could reflect functional conservation, while allowing for immune evasion through sequence variation. These structures are the first described for the S-layer of a bacterial pathogen, and provide insights into the assembly and biogenesis of the S-layer. | ||
| - | |||
| - | Structural insights into the molecular organization of the S-layer from Clostridium difficile.,Fagan RP, Albesa-Jove D, Qazi O, Svergun DI, Brown KA, Fairweather NF Mol Microbiol. 2009 Mar;71(5):1308-22. Epub 2009 Jan 29. PMID:19183279<ref>PMID:19183279</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3cvz" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Clostridioides difficile]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Albesa-Jove | + | [[Category: Albesa-Jove D]] |
| - | [[Category: Fagan | + | [[Category: Fagan R]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Structural insights into the molecular organization of the S-layer from Clostridium difficile
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