A combination of structural MS methods, molecular dynamics and smFRET was used to study the conformational dynamics and client binding of the chaperone SurA.
SurA is a key player in the assembly of outer membrane proteins in gram negative bacteria.
SurA recognises outer membrane proteins in the periplasm and transports them to the bacterial outer membrane. Without SurA, the delivery pipeline is broken and the wall cannot be built correctly. Now that we know how SurA works, we can develop molecules that interrupt this process, which can be used to destroy pathogenic bacteria