2Y2T

E. coli CsgC in reduced form

Summary for 2Y2T

• Entry DOI: 10.2210/pdb2y2t/pdb
• Related: 2Y2Y
• Descriptor: CURLI PRODUCTION PROTEIN CSGC (2 entities in total)
• Functional Keywords: chaperone, cell adhesion, biofilm, redox, cxc, oxidoreductase, immunoglobulin
• Biological source: ESCHERICHIA COLI O157\:H7 STR. EC4115
• Total number of polymer chains: 1
• Total formula weight: 12212.69

Authors

Taylor, J.D.,Salgado, P.S.,Cota, E.,Matthews, S.J. (deposition date: 2010-12-16, release date: 2011-09-21, Last modification date: 2024-05-08)

Primary citation

Taylor, J.D.,Zhou, Y.,Salgado, P.S.,Patwardhan, A.,Mcguffie, M.,Pape, T.,Grabe, G.,Ashman, E.,Constable, S.C.,Simpson, P.J.,Lee, W.C.,Cota, E.,Chapman, M.R.,Matthews, S.J.
Atomic Resolution Insights Into Curli Fiber Biogenesis.
Structure, 19:1307-, 2011

PubMed 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.

PubMed: 21893289
DOI: 10.1016/J.STR.2011.05.015

Experimental method

X-RAY DIFFRACTION (2.3 Å)