3PYW

The structure of the SLH domain from B. anthracis surface array protein at 1.8A

Summary for 3PYW

• Entry DOI: 10.2210/pdb3pyw/pdb
• Descriptor: S-layer protein sap, SULFATE ION (3 entities in total)
• Functional Keywords: slh-domains, polysaccharide binding, gst-slh, cell wall, structural genomics, psi-biology, protein structure initiative, midwest center for structural genomics, mcsg, polysaccharide, s-layer, structural protein
• Biological source: Bacillus anthracis (anthrax)
• Cellular location: Secreted, cell wall, S-layer: P49051
• Total number of polymer chains: 1
• Total formula weight: 22012.84

Authors

Zhang, R.,Wilton, R.,Kern, J.,Joachimiak, A.,Schneewind, O.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2010-12-13, release date: 2011-04-27, Last modification date: 2024-02-21)

Primary citation

Kern, J.,Wilton, R.,Zhang, R.,Binkowski, T.A.,Joachimiak, A.,Schneewind, O.
Structure of Surface Layer Homology (SLH) Domains from Bacillus anthracis Surface Array Protein.
J.Biol.Chem., 286:26042-26049, 2011

PubMed Abstract: 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 α-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.

PubMed: 21572039
DOI: 10.1074/jbc.M111.248070

Experimental method

X-RAY DIFFRACTION (1.8 Å)