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

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7 Citations (Scopus)

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 angstrom resolution and belong to space group P1 with a unit cell containing a predicted 16 molecules per asymmetric unit.
Original languageEnglish
Pages (from-to)1349-1353
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Publication statusPublished - 1 Dec 2013

Keywords

  • ESCHERICHIA-COLI
  • outer membrane
  • protein export
  • FIBRONECTIN-BINDING

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