文章基本信息

标题：Intramolecular amide bonds stabilize pili on the surface of bacilli
本地全文：下载
作者：Jonathan M. Budzik ; Catherine B. Poor ; Kym F. Faull 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2009
卷号：106
期号：47
页码：19992-19997
DOI：10.1073/pnas.0910887106
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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 (CNA2 and CNA3) 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 CNA1, 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.
关键词：CNA B domain ; jelly roll domain ; protease resistance ; sortase