2iou

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

spinqualitylabelsall models 2iou, resolution 3.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2iou is a 8 chain structure with sequence from Bordetella bronchiseptica RB50 and Bordetella virus BPP1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.16Å Ligands: MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FIBD_BPBPP Tail fiber protein located at the distal ends of the fibers that binds to the adhesion receptors on the host surface, thereby determining the host range. The phage can alter its tropism by modifying this protein. Variants are expressed through a diversity-generating retroelement (DGR) that creates mutant copies of a template repeat and replaces the end of the tail fiber receptor-binding protein with these sequences, thus changing the host range. Milliards of variants of the fiber receptor-binding protein can be created with this system. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Selective ligand recognition by a diversity-generating retroelement variable protein.,Miller JL, Le Coq J, Hodes A, Barbalat R, Miller JF, Ghosh P PLoS Biol. 2008 Jun 3;6(6):e131. PMID:18532877 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pertussis toxin

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