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TitleSupramolecular tholos-like architecture constituted by archaeal proteins without functional annotation.
Journal, issue, pagesSci Rep, Vol. 10, Issue 1, Page 1540, Year 2020
Publish dateJan 30, 2020
AuthorsMaho Yagi-Utsumi / Arunima Sikdar / Chihong Song / Jimin Park / Rintaro Inoue / Hiroki Watanabe / Raymond N Burton-Smith / Toshiya Kozai / Tatsuya Suzuki / Atsuji Kodama / Kentaro Ishii / Hirokazu Yagi / Tadashi Satoh / Susumu Uchiyama / Takayuki Uchihashi / Keehyoung Joo / Jooyoung Lee / Masaaki Sugiyama / Kazuyoshi Murata / Koichi Kato /
PubMed AbstractEuryarchaeal genomes encode proteasome-assembling chaperone homologs, PbaA and PbaB, although archaeal proteasome formation is a chaperone-independent process. Homotetrameric PbaB functions as a ...Euryarchaeal genomes encode proteasome-assembling chaperone homologs, PbaA and PbaB, although archaeal proteasome formation is a chaperone-independent process. Homotetrameric PbaB functions as a proteasome activator, while PbaA forms a homopentamer that does not interact with the proteasome. Notably, PbaA forms a complex with PF0014, an archaeal protein without functional annotation. In this study, based on our previous research on PbaA crystal structure, we performed an integrative analysis of the supramolecular structure of the PbaA/PF0014 complex using native mass spectrometry, solution scattering, high-speed atomic force microscopy, and electron microscopy. The results indicated that this highly thermostable complex constitutes ten PbaA and ten PF0014 molecules, which are assembled into a dumbbell-shaped structure. Two PbaA homopentameric rings correspond to the dumbbell plates, with their N-termini located outside of the plates and C-terminal segments left mobile. Furthermore, mutant PbaA lacking the mobile C-terminal segment retained the ability to form a complex with PF0014, allowing 3D modeling of the complex. The complex shows a five-column tholos-like architecture, in which each column comprises homodimeric PF0014, harboring a central cavity, which can potentially accommodate biomacromolecules including proteins. Our findings provide insight into the functional roles of Pba family proteins, offering a novel framework for designing functional protein cages.
External linksSci Rep / PubMed:32001743 / PubMed Central
MethodsEM (single particle)
Resolution7.3 Å
Structure data

EMDB-0755:
Recombinant Pyrococcus furiosus PbaA/PF0014 with 30 residue C-terminal truncation.
Method: EM (single particle) / Resolution: 7.3 Å

Source
  • Pyrococcus furiosus (archaea)

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