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Polymorphic Self-Assembly with Procedural Flexibility for Monodisperse Quaternary Protein Structures of DegQ Enzymes

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Title
Polymorphic Self-Assembly with Procedural Flexibility for Monodisperse Quaternary Protein Structures of DegQ Enzymes
Author(s)
Jeon, Hanul; Ah-reum Han; Oh, Sangmin; Park, Jin-Gyeong; Namkoong, Myeong; Bang, Kyeong-Mi; Ho Min Kim; Kim, Nak-Kyoon; Hwang, Kwang Yeon; Hur, Kahyun; Lee, Bong-Jin; Heo, Jeongyun; Kim, Sehoon; Song, Hyun Kyu; Cho, Hyesung; Lee, In-Gyun
Publication Date
2024-05
Journal
Advanced Materials, v.36, no.19
Publisher
WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Abstract
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. © 2024 The Authors. Advanced Materials published by Wiley-VCH GmbH.
URI
https://pr.ibs.re.kr/handle/8788114/15146
DOI
10.1002/adma.202308837
ISSN
0935-9648
Appears in Collections:
Pioneer Research Center for Biomolecular and Cellular Structure(바이오분자 및 세포구조 연구단) > Protein Communication Group(단백질 커뮤니케이션 그룹) > 1. Journal Papers (저널논문)
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