Scientists uncover 'superfamily' of bacterial predator proteins
UNIVERSITY OF BIRMINGHAM, JUL 7 – The discovery of PopA reveals a unique membrane-trapping structure in bacterial predator proteins, expanding knowledge of outer membrane proteins and their biological roles.
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A porin-like protein used by bacterial predators defines a wider lipid-trapping superfamily
Outer membrane proteins (OMPs) define the surface biology of Gram-negative bacteria, with roles in adhesion, transport, catalysis and signalling. Specifically, porin beta-barrels are common diffusion channels, predominantly monomeric/trimeric in nature. Here we show that the major OMP of the bacterial predator Bdellovibrio bacteriovorus, PopA, differs from this architecture, forming a pentameric porin-like superstructure. Our X-ray and cryo-EM s…
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