2IOU
Major Tropism Determinant P1 (Mtd-P1) Variant Complexed with Bordetella brochiseptica Virulence Factor Pertactin extracellular domain (Prn-E).
Summary for 2IOU
| Entry DOI | 10.2210/pdb2iou/pdb |
| Related | 1DAB 1YU0 |
| Descriptor | Major Tropism Determinant P1, Pertactin Extracellular Domain, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | mtd; prn; pertactin, viral protein-membrane protein complex, viral protein/membrane protein |
| Biological source | Bordetella phage BPP-1 More |
| Cellular location | Virion: Q775D6 Pertactin autotransporter: Periplasm . Outer membrane protein P. Pertactin translocator: Cell outer membrane ; Multi-pass membrane protein : Q03035 |
| Total number of polymer chains | 8 |
| Total formula weight | 343298.42 |
| Authors | Miller, J.L.,Ghosh, P. (deposition date: 2006-10-10, release date: 2007-10-23, Last modification date: 2023-08-30) |
| Primary citation | 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 Cited by 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: 18532877DOI: 10.1371/journal.pbio.0060131 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.16 Å) |
Structure validation
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