To study the functional mechanism of AAA+ metalloprotease from Aquifex aeolicus
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下载链接：
https://doi.esrf.fr/10.15151/ESRF-ES-2228385958
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资源简介：
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.
提供机构：
ESRF, 71 avenue des Martyrs, CS 40220, 38043 Grenoble Cedex 9, France; Koeln University, Baumann Laboratory, Institut fuer Biochemie, Zuelpicher Strasse 47, 50674 Koeln, Germany
创建时间：
2028-01-01
