5VAE
Crystal structure of accessory secretion protein 1 and 3
5VAE の概要
| エントリーDOI | 10.2210/pdb5vae/pdb |
| 関連するPDBエントリー | 5vaf |
| 分子名称 | Accessory Sec system protein Asp1, Accessory Sec system protein Asp3 (3 entities in total) |
| 機能のキーワード | o-glycosylation; bacterial adhesin; accessory secretion., cell adhesion |
| 由来する生物種 | Streptococcus gordonii 詳細 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 330033.33 |
| 構造登録者 | |
| 主引用文献 | Chen, Y.,Bensing, B.A.,Seepersaud, R.,Mi, W.,Liao, M.,Jeffrey, P.D.,Shajahan, A.,Sonon, R.N.,Azadi, P.,Sullam, P.M.,Rapoport, T.A. Unraveling the sequence of cytosolic reactions in the export of GspB adhesin fromStreptococcus gordonii. J. Biol. Chem., 293:5360-5373, 2018 Cited by PubMed Abstract: Many pathogenic bacteria, including , possess a pathway for the cellular export of a single serine-rich-repeat protein that mediates the adhesion of bacteria to host cells and the extracellular matrix. This adhesin protein is -glycosylated by several cytosolic glycosyltransferases and requires three accessory Sec proteins (Asp1-3) for export, but how the adhesin protein is processed for export is not well understood. Here, we report that the adhesin GspB is sequentially -glycosylated by three enzymes (GtfA/B, Nss, and Gly) that attach -acetylglucosamine and glucose to Ser/Thr residues. We also found that modified GspB is transferred from the last glycosyltransferase to the Asp1/2/3 complex. Crystal structures revealed that both Asp1 and Asp3 are related to carbohydrate-binding proteins, suggesting that they interact with carbohydrates and bind glycosylated adhesin, a notion that was supported by further analyses. We further observed that Asp1 also has an affinity for phospholipids, which is attenuated by Asp2. In summary, our findings support a model in which the GspB adhesin is sequentially glycosylated by GtfA/B, Nss, and Gly and then transferred to the Asp1/2/3 complex in which Asp1 mediates the interaction of the Asp1/2/3 complex with the lipid bilayer for targeting of matured GspB to the export machinery. PubMed: 29462788DOI: 10.1074/jbc.RA117.000963 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.106 Å) |
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