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Atomic resolution Insights into Curli Fiber Biogenesis

Lookup NU author(s): Professor Paula SalgadoORCiD

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This is the final published version of an article that has been published in its final definitive form by Cell Press, 2011.

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Abstract

Bacteria produce functional amyloid fibers called curli in a controlled, noncytotoxic manner. These extracellular fimbriae enable biofilm formation and promote pathogenicity. Understanding curli biogenesis is important for appreciating microbial lifestyles and will offer clues as to how disease-associated human amyloid formation might be ameliorated. Proteins encoded by the curli specific genes (csgA-G) are required for curli production. We have determined the structure of CsgC and derived the first structural model of the outer-membrane subunit translocator CsgG. Unexpectedly, CsgC is related to the N-terminal domain of DsbD, both in structure and oxido-reductase capability. Furthermore, we show that CsgG belongs to the nascent class of helical outer-membrane macromolecular exporters. A cysteine in a CsgG transmembrane helix is a potential target of CsgC, and mutation of this residue influences curli assembly. Our study provides the first high-resolution structural insights into curli biogenesis.

Publication metadata

Author(s): Taylor JD, Zhou Y, Salgado PS, Patwardhan A, McGuffie M, Pape T, Grabe G, Ashman E, Constable SC, Simpson PJ, Lee W, Cota E, Chapman MR, Matthews SJ

Publication type: Article

Publication status: Published

Journal: Structure

Year: 2011

Volume: 19

Issue: 9

Pages: 1307-1316

Print publication date: 07/09/2011

Date deposited: 08/11/2012

ISSN (print): 0969-2126

ISSN (electronic): 1878-4186

Publisher: Cell Press

URL: http://dx.doi.org/10.1016/j.str.2011.05.015

DOI: 10.1016/j.str.2011.05.015

PubMed id: 21893289

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