To study the functional mechanism of AAA+ metalloprotease from Aquifex aeolicus

AAA+ (ATPases Associated with diverse cellular Activities) proteins undergo complex conformational changes driven by ATP binding and hydrolysis. Cryo-electron microscopy (cryo-EM), combined with nucleotide analogues such as ATPγS, ADP, or AMP-PNP, allows the capture of these dynamic proteins in distinct mechanochemical states. By comparing these snapshots, cryo-EM provides mechanistic insight into how nucleotide state coordinates structural transitions, substrate engagement, and force generation, shedding light on the core principles of AAA+ protein function. We have chosen the AAA+ protein from Aquifex aeolicus. Furthermore we would like to study the structure of this protein with a nanobody to stabilize the flexibility observed in the ATPase part of the protein.