Crystal Structure of p97 N-D1 Hexamer in Complex with p47 UBX Domain
- Authors
- Nguyen, Thang Quyet; Kang, Wonchull
- Issue Date
- Feb-2024
- Publisher
- Korean Chemical Society
- Keywords
- Crystal structure; p47; p97; Stoichiometry; UBX
- Citation
- Journal of the Korean Chemical Society, v.68, no.1, pp 25 - 31
- Pages
- 7
- Journal Title
- Journal of the Korean Chemical Society
- Volume
- 68
- Number
- 1
- Start Page
- 25
- End Page
- 31
- URI
- https://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/49263
- DOI
- 10.5012/jkcs.2024.68.1.25
- ISSN
- 1017-2548
2234-8530
- Abstract
- The p97 adenosine triphosphatase is a key player in protein homeostasis, responsible for unfolding ubiquitylated substrates. It engages with various adaptor proteins through its N-terminal domain, with the p97-p47 complex attracting particular attention for its involvement in membrane remodeling. Although the structures of p97 in complex with the Ubiquitin regulatory X (UBX) domain from various adaptors have been reported, the stoichiometry is conflicting. Here, we report the crystal structure of the p97 N-D1 hexamer in complex with the p47 UBX domain at a resolution of 2.7 Å. The structure reveals a stoichiometry of 6:6 between the p97 N-D1 and the p47 UBX domain. These findings provide valuable insights into the binding stoichiometry of p97 N-D1 and p47 UBX domain, which are crucial for understanding the role of p97 and adaptor proteins in cellular processes such as the ubiquitin-proteasome pathway, membrane fusion, and cell cycle regulation. © 2024 Korean Chemical Society. All rights reserved.
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