Jeon, Hanul Han, Ah-reum Oh, Sangmin Park, Jin-Gyeong Namkoong, Myeong Bang, Kyeong-Mi Kim, Ho Min Kim, Nak-Kyoon Hwang, Kwang Yeon Hur, Kahyun Lee, Bong-Jin Heo, Jeongyun Kim, Sehoon Song, Hyun Kyu Cho, Hyesung Lee, In-Gyun 2024-03-13T07:30:22Z 2024-03-13T07:30:22Z 2024-03-13 2024-05 0935-9648 https://pubs.kist.re.kr/handle/201004/149464 As large molecular tertiary structures, some proteins can act as small robots that find, bind, and chaperone target protein clients, showing the potential to serve as smart building blocks in self-assembly fields. Instead of using such intrinsic functions, most self-assembly methodologies for proteins aim for de novo-designed structures with accurate geometric assemblies, which can limit procedural flexibility. Here, a strategy enabling polymorphic clustering of quaternary proteins, exhibiting simplicity and flexibility of self-assembling paths for proteins in forming monodisperse quaternary cage particles is presented. It is proposed that the enzyme protomer DegQ, previously solved at low resolution, may potentially be usable as a threefold symmetric building block, which can form polyhedral cages incorporated by the chaperone action of DegQ in the presence of protein clients. To obtain highly monodisperse cage particles, soft, and hence, less resistive client proteins, which can program the inherent chaperone activity of DegQ to efficient formations of polymorphic cages, depending on the size of clients are utilized. By reconstructing the atomic resolution cryogenic electron microscopy DegQ structures using obtained 12- and 24-meric clusters, the polymorphic clustering of DegQ enzymes is validated in terms of soft and rigid domains, which will provide effective routes for protein self-assemblies with procedural flexibility. English WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim Polymorphic Self-Assembly with Procedural Flexibility for Monodisperse Quaternary Protein Structures of DegQ Enzymes Article 10.1002/adma.202308837 1 Advanced Materials, v.36, no.19 Advanced Materials 36 19 Y scie scopus 001175740400001 2-s2.0-85186240667 Chemistry, Multidisciplinary Chemistry, Physical Nanoscience & Nanotechnology Materials Science, Multidisciplinary Physics, Applied Physics, Condensed Matter Chemistry Science & Technology - Other Topics Materials Science Physics Article POLYHEDRA DNA DESIGN CAGE procedural flexibility quaternary protein structures self-assemblies