2IOU

Major Tropism Determinant P1 (Mtd-P1) Variant Complexed with Bordetella brochiseptica Virulence Factor Pertactin extracellular domain (Prn-E).

2IOU の概要

• エントリーDOI: 10.2210/pdb2iou/pdb
• 関連するPDBエントリー: 1DAB 1YU0
• 分子名称: Major Tropism Determinant P1, Pertactin Extracellular Domain, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: mtd; prn; pertactin, viral protein-membrane protein complex, viral protein/membrane protein
• 由来する生物種: Bordetella phage BPP-1; 詳細
• 細胞内の位置: Virion: Q775D6; Pertactin autotransporter: Periplasm . Outer membrane protein P. Pertactin translocator: Cell outer membrane ; Multi-pass membrane protein : Q03035
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 343298.42

構造登録者

Miller, J.L.,Ghosh, P. (登録日: 2006-10-10, 公開日: 2007-10-23, 最終更新日: 2023-08-30)

主引用文献

Miller, J.L.,Le Coq, J.,Hodes, A.,Barbalat, R.,Miller, J.F.,Ghosh, P.
Selective Ligand Recognition by a Diversity-Generating Retroelement Variable Protein
Plos Biol., 6:e131-e131, 2008

PubMed Abstract: Diversity-generating retroelements (DGRs) recognize novel ligands through massive protein sequence variation, a property shared uniquely with the adaptive immune response. Little is known about how recognition is achieved by DGR variable proteins. Here, we present the structure of the Bordetella bacteriophage DGR variable protein major tropism determinant (Mtd) bound to the receptor pertactin, revealing remarkable adaptability in the static binding sites of Mtd. Despite large dissimilarities in ligand binding mode, principles underlying selective recognition were strikingly conserved between Mtd and immunoreceptors. Central to this was the differential amplification of binding strengths by avidity (i.e., multivalency), which not only relaxed the demand for optimal complementarity between Mtd and pertactin but also enhanced distinctions among binding events to provide selectivity. A quantitatively similar balance between complementarity and avidity was observed for Bordetella bacteriophage DGR as occurs in the immune system, suggesting that variable repertoires operate under a narrow set of conditions to recognize novel ligands.

PubMed: 18532877
DOI: 10.1371/journal.pbio.0060131

実験手法

X-RAY DIFFRACTION (3.16 Å)