I was just looking at grant app from Jan that wasn't funded and I was tickled by this formatting weirdness that described it as "100% unsuccessful".

As if to say, "It wasn't even a *little bit* successful, so don't get any ideas!"

It was completely maxed out in its level of unsuccessfulness!

Therefore, we believe we have identified a new class of SBP-dependent secondary active transporter. And this is what it looks like when we model the heterotetramer of BP0403 and GltS. (9/9)

While GltS is part of an unrelated family, like TRAP transporters, we predict that it uses an elevator mechanism based on the structural model, but unlike TRAP transporters it is dimeric, so it is more like our old friend VcINDY from the DASS family, which uses an elevator-like mechanism. (7/9)

As if this wasn’t interesting enough, genome context analysis of BP0403 revealed no TRAP membrane component gene. Instead, what we found was a gene encoding GltS, which is not at all related to TRAP transporters and is part of the glutamate sodium symporter (ESS) family. (6/9)

By making BP0403 truncations, we showed that the helical domain was indeed responsible for dimerisation. Lily then showed that the SBP binds L-glutamate (a key pertussis metabolite) using DSF, and with help from @socobiodtp.bsky.social PhD student Joseph Davies, showed it has a nM affinity. (5/9)

Lily demonstrated that BP0403 forms a stable dimer – a very unusually occurrence for a TRAP SBP, and modelling the dimeric structure predicted that the dimeric interface was entirely formed by the helical region. (4/9)

Rather than being a single domain SBP like all other characterised TRAP SBPs, BP0403 is nearly twice the length and consists of 3 distinct domains; a globular N-terminal domain, a helical region and a classical SBP domain a the C-terminus. (3/9)