3PYW
The structure of the SLH domain from B. anthracis surface array protein at 1.8A
3PYW の概要
| エントリーDOI | 10.2210/pdb3pyw/pdb |
| 分子名称 | S-layer protein sap, SULFATE ION (3 entities in total) |
| 機能のキーワード | 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 |
| 由来する生物種 | Bacillus anthracis (anthrax) |
| 細胞内の位置 | Secreted, cell wall, S-layer: P49051 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 22012.84 |
| 構造登録者 | Zhang, R.,Wilton, R.,Kern, J.,Joachimiak, A.,Schneewind, O.,Midwest Center for Structural Genomics (MCSG) (登録日: 2010-12-13, 公開日: 2011-04-27, 最終更新日: 2024-02-21) |
| 主引用文献 | 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 Cited by 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: 21572039DOI: 10.1074/jbc.M111.248070 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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