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3pyw
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| - | [[ | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3pyw]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PYW FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
| + | <tr><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 anthracis])</td></tr> | ||
| + | <tr><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://www.rcsb.org/pdb/explore.do?structureId=3pyw RCSB], [http://www.ebi.ac.uk/pdbsum/3pyw PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
[[Category: Joachimiak, A.]] | [[Category: Joachimiak, A.]] | ||
Revision as of 06:53, 9 June 2014
The structure of the SLH domain from B. anthracis surface array protein at 1.8A
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Categories: Bacillus anthracis | Joachimiak, A. | Kern, J. | MCSG, Midwest Center for Structural Genomics. | Schneewind, O. | Wilton, R. | Zhang, R. | Cell wall | Gst-slh | Mcsg | Midwest center for structural genomic | Polysaccharide | Polysaccharide binding | Protein structure initiative | Psi-biology | S-layer | Slh-domain | Structural genomic | Structural protein
