3ino | pdb_00003ino

1.95A Resolution Structure of Protective Antigen Domain 4

spinqualitylabelsall models 3ino, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ino is a 2 chain structure with sequence from "bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: pagA, pag, pXO1-110, BXA0164, GBAA_pXO1_0164 ("Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PAG_BACAN] One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. PA binds to a receptor (ATR) in sensitive eukaryotic cells, thereby facilitating the translocation of the enzymatic toxin components, edema factor and lethal factor, across the target cell membrane. PA associated with LF causes death when injected, PA associated with EF produces edema. PA induces immunity to infection with anthrax. Publication Abstract from PubMed Domain 4 of the anthrax protective antigen (PA) plays a key role in cellular receptor recognition as well as in pH-dependent pore formation. We present here the 1.95 A crystal structure of domain 4, which adopts a fold that is identical to that observed in the full-length protein. We have also investigated the structural properties of the isolated domain 4 as a function of pH, as well as the pH-dependence on binding to the von Willebrand factor A domain of capillary morphogenesis protein 2 (CMG2). Our results provide evidence that the isolated domain 4 maintains structure and interactions with CMG2 at pH 5, a pH that is known to cause release of the receptor on conversion of the heptameric prepore (PA(63))(7) to a membrane-spanning pore. Our results suggest that receptor release is not driven solely by a pH-induced unfolding of domain 4. Domain 4 of the anthrax protective antigen maintains structure and binding to the host receptor CMG2 at low pH.,Williams AS, Lovell S, Anbanandam A, El-Chami R, Bann JG Protein Sci. 2009 Nov;18(11):2277-86. PMID:19722284 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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