Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 106, Issue 47, Pages 19992-19997Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0910887106
Keywords
CNA B domain; jelly roll domain; protease resistance; sortase
Categories
Funding
- US Public Health Service [AI38897, AI074658]
- National Institutes of Health [GM07281]
- National Science Foundation
- Region V Great Lakes'' Regional Center of Excellence in Biodefense and Emerging Infectious Diseases Consortium (NIAID) [Award 1-U54-AI-057153]
- United States Department of Energy
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Gram-positive bacteria elaborate pili and do so without the participation of folding chaperones or disulfide bond catalysts. Sortases, enzymes that cut pilin precursors, form covalent bonds that link pilin subunits and assemble pili on the bacterial surface. We determined the x-ray structure of BcpA, the major pilin subunit of Bacillus cereus. The BcpA precursor encompasses 2 Ig folds (CNA(2) and CNA(3)) and one jelly-roll domain (XNA) each of which synthesizes a single intramolecular amide bond. A fourth amide bond, derived from the Ig fold of CNA(1), is formed only after pilin subunits have been incorporated into pili. We report that the domains of pilin precursors have evolved to synthesize a discrete sequence of intramolecular amide bonds, thereby conferring structural stability and protease resistance to pili.
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