1WCK
Crystal structure of the C-terminal domain of BclA, the major antigen of the exosporium of the Bacillus anthracis spore.
Summary for 1WCK
| Entry DOI | 10.2210/pdb1wck/pdb |
| Descriptor | BCLA PROTEIN, CACODYLATE ION (3 entities in total) |
| Functional Keywords | collagen-like protein, bacterial surface antigen, jelly-roll topology, structural protein |
| Biological source | BACILLUS ANTHRACIS |
| Total number of polymer chains | 1 |
| Total formula weight | 21534.00 |
| Authors | Rety, S.,Salamitou, S.,Augusto, L.A.,Chaby, R.,Lehegarat, F.,Lewit-Bentley, A. (deposition date: 2004-11-17, release date: 2005-10-25, Last modification date: 2024-10-16) |
| Primary citation | Rety, S.,Salamitou, S.,Garcia-Verdugo, I.,Hulmes, D.J.,Lehegarat, F.,Chaby, R.,Lewit-Bentley, A. The Crystal Structure of the Bacillus Anthracis Spore Surface Protein Bcla Shows Remarkable Similarity to Mammalian Proteins. J.Biol.Chem., 280:43073-, 2005 Cited by PubMed Abstract: 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. PubMed: 16249180DOI: 10.1074/JBC.M510087200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.36 Å) |
Structure validation
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