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| | <SX load='6t72' size='340' side='right' viewer='molstar' caption='[[6t72]], [[Resolution|resolution]] 3.70Å' scene=''> | | <SX load='6t72' size='340' side='right' viewer='molstar' caption='[[6t72]], [[Resolution|resolution]] 3.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6t72]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cauvc Cauvc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T72 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6T72 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6t72]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides_CB15 Caulobacter vibrioides CB15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T72 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MRH:alpha-N-Acetylperosamine'>MRH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rsaA, CC_1007 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=190650 CAUVC])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MRH:4-acetamido-4,6-dideoxy-alpha-D-mannopyranose'>MRH</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=6t72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t72 OCA], [http://pdbe.org/6t72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t72 RCSB], [http://www.ebi.ac.uk/pdbsum/6t72 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t72 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=6t72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t72 OCA], [https://pdbe.org/6t72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t72 RCSB], [https://www.ebi.ac.uk/pdbsum/6t72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t72 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SLAP_CAUVC SLAP_CAUVC]] The S-layer is a paracrystalline mono-layered assembly of proteins which coats the surface of bacteria. Probably acts as a physical barrier to parasites and lytic enzymes. | + | [https://www.uniprot.org/uniprot/SLAP_CAUVC SLAP_CAUVC] The S-layer is a paracrystalline mono-layered assembly of proteins which coats the surface of bacteria. Probably acts as a physical barrier to parasites and lytic enzymes. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Cauvc]] | + | [[Category: Caulobacter vibrioides CB15]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bharat, T A.M]] | + | [[Category: Bharat TAM]] |
| - | [[Category: Kuegelgen, A von]] | + | [[Category: Von Kuegelgen A]] |
| - | [[Category: S-layer lps rsaa]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
SLAP_CAUVC The S-layer is a paracrystalline mono-layered assembly of proteins which coats the surface of bacteria. Probably acts as a physical barrier to parasites and lytic enzymes.
Publication Abstract from PubMed
Most bacterial and all archaeal cells are encapsulated by a paracrystalline, protective, and cell-shape-determining proteinaceous surface layer (S-layer). On Gram-negative bacteria, S-layers are anchored to cells via lipopolysaccharide. Here, we report an electron cryomicroscopy structure of the Caulobacter crescentus S-layer bound to the O-antigen of lipopolysaccharide. Using native mass spectrometry and molecular dynamics simulations, we deduce the length of the O-antigen on cells and show how lipopolysaccharide binding and S-layer assembly is regulated by calcium. Finally, we present a near-atomic resolution in situ structure of the complete S-layer using cellular electron cryotomography, showing S-layer arrangement at the tip of the O-antigen. A complete atomic structure of the S-layer shows the power of cellular tomography for in situ structural biology and sheds light on a very abundant class of self-assembling molecules with important roles in prokaryotic physiology with marked potential for synthetic biology and surface-display applications.
In Situ Structure of an Intact Lipopolysaccharide-Bound Bacterial Surface Layer.,von Kugelgen A, Tang H, Hardy GG, Kureisaite-Ciziene D, Brun YV, Stansfeld PJ, Robinson CV, Bharat TAM Cell. 2020 Jan 23;180(2):348-358.e15. doi: 10.1016/j.cell.2019.12.006. Epub 2019 , Dec 26. PMID:31883796[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ von Kugelgen A, Tang H, Hardy GG, Kureisaite-Ciziene D, Brun YV, Stansfeld PJ, Robinson CV, Bharat TAM. In Situ Structure of an Intact Lipopolysaccharide-Bound Bacterial Surface Layer. Cell. 2020 Jan 23;180(2):348-358.e15. doi: 10.1016/j.cell.2019.12.006. Epub 2019 , Dec 26. PMID:31883796 doi:http://dx.doi.org/10.1016/j.cell.2019.12.006
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