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| | ==The structure of the SLH domain from B. anthracis surface array protein at 1.8A== | | ==The structure of the SLH domain from B. anthracis surface array protein at 1.8A== |
| - | <StructureSection load='3pyw' size='340' side='right' caption='[[3pyw]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='3pyw' size='340' side='right'caption='[[3pyw]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pyw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PYW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3pyw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PYW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAS0841, BA_0885, GBAA_0885, GI:49183865, sap ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 "Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pyw OCA], [http://pdbe.org/3pyw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pyw RCSB], [http://www.ebi.ac.uk/pdbsum/3pyw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pyw 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=3pyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pyw OCA], [https://pdbe.org/3pyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pyw RCSB], [https://www.ebi.ac.uk/pdbsum/3pyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pyw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SLAP1_BACAN SLAP1_BACAN]] The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria. | + | [https://www.uniprot.org/uniprot/SLAP1_BACAN SLAP1_BACAN] The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria. |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Surface (S)-layers, para-crystalline arrays of protein, are deposited in the envelope of most bacterial species. These surface organelles are retained in the bacterial envelope through the non-covalent association of proteins with cell wall carbohydrates. Bacillus anthracis, a Gram-positive pathogen, produces S-layers of the protein Sap, which uses three consecutive repeats of the surface-layer homology (SLH) domain to engage secondary cell wall polysaccharides (SCWP). Using x-ray crystallography, we reveal here the structure of these SLH domains, which assume the shape of a three-prong spindle. Each SLH domain contributes to a three-helical bundle at the spindle base, whereas another alpha-helix and its connecting loops generate the three prongs. The inter-prong grooves contain conserved cationic and anionic residues, which are necessary for SLH domains to bind the B. anthracis SCWP. Modeling experiments suggest that the SLH domains of other S-layer proteins also fold into three-prong spindles and capture bacterial envelope carbohydrates by a similar mechanism.
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| - | Structure of Surface Layer Homology (SLH) Domains from Bacillus anthracis Surface Array Protein.,Kern J, Wilton R, Zhang R, Binkowski TA, Joachimiak A, Schneewind O J Biol Chem. 2011 Jul 22;286(29):26042-9. Epub 2011 May 13. PMID:21572039<ref>PMID:21572039</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3pyw" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Joachimiak, A]] | + | [[Category: Bacillus anthracis]] |
| - | [[Category: Kern, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]] | + | [[Category: Joachimiak A]] |
| - | [[Category: Schneewind, O]] | + | [[Category: Kern J]] |
| - | [[Category: Wilton, R]] | + | [[Category: Schneewind O]] |
| - | [[Category: Zhang, R]] | + | [[Category: Wilton R]] |
| - | [[Category: Cell wall]] | + | [[Category: Zhang R]] |
| - | [[Category: Gst-slh]]
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| - | [[Category: Mcsg]]
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| - | [[Category: Polysaccharide]]
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| - | [[Category: Polysaccharide binding]]
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| - | [[Category: PSI, Protein structure initiative]]
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| - | [[Category: Psi-biology]]
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| - | [[Category: S-layer]]
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| - | [[Category: Slh-domain]]
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| - | [[Category: Structural protein]]
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