Crystallization and preliminary X-ray crystallographic analysis of the curli transporter CsgG.

TitleCrystallization and preliminary X-ray crystallographic analysis of the curli transporter CsgG.
Publication TypeJournal Article
Year of Publication2013
AuthorsGoyal, P., N. Van Gerven, W. Jonckheere, and H. Remaut
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume69
IssuePt 12
Pagination1349-53
Date Published2013 Dec
ISSN1744-3091
KeywordsCrystallization, Crystallography, X-Ray, Escherichia coli, Escherichia coli Proteins, Gene Expression, Lipoproteins, Protein Multimerization, Recombinant Proteins
Abstract

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 P1 with a unit cell containing a predicted 16 molecules per asymmetric unit.

DOI10.1107/S1744309113028054
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID24316827
PubMed Central IDPMC3855717
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