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

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.

SUBMITTER: Goyal P

PROVIDER: S-EPMC3855717 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature

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

Goyal Parveen P Goyal Parveen P Van Gerven Nani N Jonckheere Wim W Remaut Han H

Acta crystallographica. Section F, Structural biology and crystallization communications 20131128 Pt 12

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 ...[more]

PMID: 24316827

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