Crystallization and preliminary X‐ray crystallographic analysis of the curli transporter CsgG. Issue 12 (1st December 2013)

• Record Type: Journal Article
• Authors: Goyal, Parveen; Van Gerven, Nani; Jonckheere, Wim; Remaut, Han
• Is Part Of: Acta crystallographica. Volume 69:Issue 12(2013:Dec.)
• Page Start: 1349
• Page End: 1353
• Publication Date: 2013-12-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113028054
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>Escherichia coli</italic> 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 <italic>P</italic>1 with a unit cell containing a predicted 16 molecules per asymmetric unit.</p> </abstract>