Open AccessCrystallization and preliminary X‐ray crystallographic analysis of the curli transporter CsgG
Author(s) -
Goyal Parveen,
Van Gerven Nani,
Jonckheere Wim,
Remaut Han
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113028054
Subject(s) - secretion , biofilm , crystallization , escherichia coli , crystallography , biophysics , bacterial outer membrane , bacteria , transporter , chemistry , extracellular , molecule , mutant , microbiology and biotechnology , biology , biochemistry , gene , genetics , organic chemistry
Gram‐negative bacteria have eight known protein secretion systems. The type‐VIII secretion system, also known as the curli biosynthesis system, is responsible for the formation of aggregative fibres known in Escherichia coli as curli. Curli are extracellular proteinaceous fibres primarily involved in bacterial biofilm formation and attachment to nonbiotic surfaces. The secretion of curli subunits depends on a dedicated lipoprotein, CsgG, which is found to form an oligomeric secretion channel in the outer membrane. A nonlipidated mutant of CsgG was expressed and crystallized in a soluble form. The crystals diffracted to 3.15 Å resolution and belong to space group P 1 with a unit cell containing a predicted 16 molecules per asymmetric unit.