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<StructureSection load='3pyw' size='340' side='right'caption='[[3pyw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3pyw' size='340' side='right'caption='[[3pyw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3pyw]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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" id="ligandDat"><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]] 1.8&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAS0841, BA_0885, GBAA_0885, GI:49183865, sap ([https://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'>[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>
<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 ==
[[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.  
[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;">
== Publication Abstract from PubMed ==
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3pyw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus anthracis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Joachimiak, A]]
[[Category: Joachimiak A]]
[[Category: Kern, J]]
[[Category: Kern J]]
[[Category: Structural genomic]]
[[Category: Schneewind O]]
[[Category: Schneewind, O]]
[[Category: Wilton R]]
[[Category: Wilton, R]]
[[Category: Zhang R]]
[[Category: Zhang, R]]
[[Category: Cell wall]]
[[Category: Gst-slh]]
[[Category: Mcsg]]
[[Category: Polysaccharide]]
[[Category: Polysaccharide binding]]
[[Category: PSI, Protein structure initiative]]
[[Category: Psi-biology]]
[[Category: S-layer]]
[[Category: Slh-domain]]
[[Category: Structural protein]]
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