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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 12(69), p. 1349-1353, 2013

DOI: 10.1107/s1744309113028054

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

Journal article published in 2013 by Parveen Goyal ORCID, Nani Van Gerven, Wim Jonckheere, Han Remaut
This paper is available in a repository.
This paper is available in a repository.

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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.