1wck

Crystal structure of the C-terminal domain of BclA, the major antigen of the exosporium of the Bacillus anthracis spore.

spinqualitylabelsall models 1wck, resolution 1.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1wck is a 1 chain structure with sequence from Bacillus anthracis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.36Å Ligands: CAC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q83WB0_BACAN 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 The lethal disease anthrax is propagated by spores of Bacillus anthracis, which can penetrate into the mammalian host by inhalation, causing a rapid progression of the disease and a mostly fatal outcome. We have solved the three-dimensional structure of the major surface protein BclA on B. anthracis spores. Surprisingly, the structure resembles C1q, the first component of complement, despite there being no sequence homology. Although most assays for C1q-like activity, including binding to C1q receptors, suggest that BclA does not mimic C1q, we show that BclA, as well as C1q, interacts with components of the lung alveolar surfactant layer. Thus, to better recognize and invade its hosts, this pathogenic soil bacterium may have evolved a surface protein whose structure is strikingly close to a mammalian protein. The crystal structure of the Bacillus anthracis spore surface protein BclA shows remarkable similarity to mammalian proteins.,Rety S, Salamitou S, Garcia-Verdugo I, Hulmes DJ, Le Hegarat F, Chaby R, Lewit-Bentley A J Biol Chem. 2005 Dec 30;280(52):43073-8. Epub 2005 Oct 25. PMID:16249180 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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