3KPT

Crystal structure of BcpA, the major pilin subunit of Bacillus cereus

Summary for 3KPT

• Entry DOI: 10.2210/pdb3kpt/pdb
• Descriptor: Collagen adhesion protein, CALCIUM ION (3 entities in total)
• Functional Keywords: intramolecular amide bond, pilin subunit, beta sheet, cell adhesion
• Biological source: Bacillus cereus ATCC 14579
• Total number of polymer chains: 2
• Total formula weight: 78970.41

Authors

Poor, C.B.,Budzik, J.M.,Schneewind, O.,He, C. (deposition date: 2009-11-16, release date: 2009-11-24, Last modification date: 2024-11-06)

Primary citation

Budzik, J.M.,Poor, C.B.,Faull, K.F.,Whitelegge, J.P.,He, C.,Schneewind, O.
Intramolecular amide bonds stabilize pili on the surface of bacilli.
Proc.Natl.Acad.Sci.USA, 106:19992-19997, 2009

PubMed Abstract: 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.

PubMed: 19903875
DOI: 10.1073/pnas.0910887106

Experimental method

X-RAY DIFFRACTION (2.102 Å)