Intramolecular amide bonds stabilize pili on the surface of bacilli

被引：62

作者：

Budzik, Jonathan M. ^{[2
]}

Poor, Catherine B. ^{[1
]}

Faull, Kym F. ^{[3
]}

Whitelegge, Julian P. ^{[3
]}

He, Chuan ^{[1
]}

Schneewind, Olaf ^{[2
]}

机构：

[1] Univ Chicago, Dept Chem, Chicago, IL 60637 USA

[2] Univ Chicago, Dept Microbiol, Chicago, IL 60637 USA

[3] Univ Calif Los Angeles, David Geffen Sch Med, Semel Inst Neurosci & Human Behav, Neuropsychiat Inst,Pasarow Mass Spectrometry Lab, Los Angeles, CA 90095 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2009年 / 106卷 / 47期

基金：

美国能源部; 美国国家卫生研究院; 美国国家科学基金会;

关键词：

CNA B domain; jelly roll domain; protease resistance; sortase; BACTERIAL OUTER-MEMBRANE; GRAM-POSITIVE BACTERIA; STAPHYLOCOCCUS-AUREUS; ISOPEPTIDE BONDS; ESCHERICHIA-COLI; STRUCTURAL BASIS; LPXTG MOTIF; PROTEINS; ADHESIN; SORTASE;

D O I：

10.1073/pnas.0910887106

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

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 (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.

引用

页码：19992 / 19997

页数：6

共 32 条

[11] Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC [J].