5MKC
Crystal structure of the RrgA Jo.In complex
5MKC の概要
エントリーDOI | 10.2210/pdb5mkc/pdb |
分子名称 | Cell wall surface anchor family protein (Jo),Cell wall surface anchor family protein (In), SULFATE ION, NICKEL (II) ION, ... (5 entities in total) |
機能のキーワード | bacteria, peptidoglycan, pilus adhesin, cross-links, folding, post-translational, isopeptide bond, biotechnology, cell adhesion |
由来する生物種 | Streptococcus pneumoniae 詳細 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 158575.82 |
構造登録者 | Bonnet, J.,Cartannaz, J.,Tourcier, G.,Contreras-Martel, C.,Kleman, J.P.,Fenel, D.,Schoehn, G.,Morlot, C.,Vernet, T.,Di Guilmi, A.M. (登録日: 2016-12-03, 公開日: 2017-03-15, 最終更新日: 2024-10-16) |
主引用文献 | Bonnet, J.,Cartannaz, J.,Tourcier, G.,Contreras-Martel, C.,Kleman, J.P.,Morlot, C.,Vernet, T.,Di Guilmi, A.M. Autocatalytic association of proteins by covalent bond formation: a Bio Molecular Welding toolbox derived from a bacterial adhesin. Sci Rep, 7:43564-43564, 2017 Cited by PubMed Abstract: Unusual intramolecular cross-links present in adhesins from Gram-positive bacteria have been used to develop a generic process amenable to biotechnology applications. Based on the crystal structure of RrgA, the Streptococcus pneumoniae pilus adhesin, we provide evidence that two engineered protein fragments retain their ability to associate covalently with high specificity, in vivo and in vitro, once isolated from the parent protein. We determined the optimal conditions for the assembly of the complex and we solved its crystal structure at 2 Å. Furthermore, we demonstrate biotechnological applications related to antibody production, nanoassembly and cell-surface labeling based on this process we named Bio Molecular Welding. PubMed: 28252635DOI: 10.1038/srep43564 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.04 Å) |
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