3pyw: Difference between revisions
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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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Proteopedia Page Contributors and Editors (what is this?)
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
