1wck
From Proteopedia
Revision as of 12:55, 20 March 2008
| |||||||
| , resolution 1.36Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF BCLA, THE MAJOR ANTIGEN OF THE EXOSPORIUM OF THE BACILLUS ANTHRACIS SPORE.
Overview
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.
About this Structure
1WCK is a Single protein structure of sequence from Bacillus anthracis. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 14:55:20 2008
