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조혜성Hyesung Cho

KIST

Adv. Mater., Feb 13 2024, | https://doi.org/10.1002/adma.202308837 Polymorphic Self-Assembly with Procedural Flexibility for Monodisperse Quaternary Protein Structures of DegQ Enzymes

Hanul Jeon^1,2, Ah-Reum Han³, Sangmin Oh ⁴, Jin-Gyeong Park ^1,2, Myeong Namkoong ⁴, Kyeong-Mi Bang^5,6, Ho Min Kim ^3,7, Nak-Kyoon Kim ⁵, Kwang Yeon Hwang ², Kahyun Hur ⁴, Bong-Jin Lee ^8,9, Jeongyun Heo ¹, Sehoon Kim ^1,10, Hyun Kyu Song ⁶, Hyesung Cho⁴, In-Gyun Lee ¹

¹Biomedical Research Division, Korea Institute of Science and Technology, 5, Hwarang-ro 14-gil, Seongbuk-gu, Seoul, 02792, Republic of Korea.

²Department of Biotechnology, Korea University, 145, Anam-ro, Seongbuk-gu, Seoul, 02841, Republic of Korea.

³Center for Biomolecular and Cellular Structure, Life Science Cluster, Institute for Basic Science (IBS), 55, Expo-ro, Daejeon, 34126, Republic of Korea.

⁴Extreme Materials Research Center, Korea Institute of Science and Technology, 5, Hwarang-ro 14-gil, Seongbuk-gu, Seoul, 02792, Republic of Korea.

⁵Advanced Analysis Center, Korea Institute of Science and Technology, 5, Hwarang-ro 14-gil Seongbuk-gu, Seoul, 02792, Republic of Korea.

⁶Department of Life Science, Korea University, ,145, Anam-ro, Seongbuk-gu, Seoul, 02841, Republic of Korea.

⁷Graduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), 291, Daehak-ro, Daejeon, 34126, Republic of Korea.

⁸The Research Institute of Pharmaceutical Science, Seoul National University, 599, Gwanak-ro, Gwanak-gu, Seoul, 08826, Republic of Korea.

⁹College of Pharmacy, Ajou University, 206, Worldcup-ro, Yeongtong-gu, Suwon-si, Gyeonggi-do, 16499, Republic of Korea.

¹⁰KU-KIST Graduate School of Converging Science and Technology, Korea University, 145, Anam-ro, Seongbuk-gu, Seoul, 02841, Republic of Korea.

CORRESPONDING AUTHORS : Hyesung Cho, In-Gyun Lee

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 could limit procedural flexibility. Here, we present a strategy enabling polymorphic clustering of quaternary proteins, exhibiting simplicity and flexibility of self-assembling paths for proteins in forming monodisperse quaternary cage particles. We propose 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, we utilize 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. By reconstructing the atomic resolution cryo-EM DegQ structures using obtained 12- and 24-meric clusters, we validate the polymorphic clustering of DegQ enzymes in terms of soft and rigid domains, which would provide effective routes for protein self-assemblies with procedural flexibility. This article is protected by copyright. All rights reserved.

논문정보

형식Research article
게재일2024년 02월 (BRIC 등록일 2024-02-15)
연구진국내 연구진
분야 의약학 > 약학

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