3KPT

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

3KPT の概要

• エントリーDOI: 10.2210/pdb3kpt/pdb
• 分子名称: Collagen adhesion protein, CALCIUM ION (3 entities in total)
• 機能のキーワード: intramolecular amide bond, pilin subunit, beta sheet, cell adhesion
• 由来する生物種: Bacillus cereus ATCC 14579
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78970.41

構造登録者

Poor, C.B.,Budzik, J.M.,Schneewind, O.,He, C. (登録日: 2009-11-16, 公開日: 2009-11-24, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.102 Å)