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Updated: Jun 11, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
The structure of Yersinia pestis Caf1 polymer in free and adjuvant bound states
Andrei Soliakov1, J Robin Harris, Allan Watkinson
1Institute for Cell and Molecular Sciences, Newcastle University, Framlington Place, Newcastle-upon-Tyne, NE2 4HH, UK.
Abstract:
Caf1 of the plague bacterium, Yersinia pestis is a polymeric virulence factor and vaccine component, formed from monomers by a donor strand exchange (DSE) mechanism. Here, EM images of Caf1 reveal flexible polymers up to 1.5 microm long (4MDa). The bead-like structures along the polymer are 5.8 + or - 1 nm long and correspond to single Caf1 proteins. Short polymers often form circles, presumably by DSE. We also provide the first images of proteins bound to alhydrogel adjuvant. Caf1, hemocyanin and anthrax PA are all resolved clearly and Caf1 exhibits adjuvant bound stretches with long intervening loops draped from the edges.
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