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  Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle

Majumder, P., Rudack, T., Beck, F., Danev, R., Pfeifer, G., Nagy, I., et al. (2019). Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle. Proceedings of the National Academy of Sciences of the United States of America, 116(2), 534-539. doi:10.1073/pnas.1817752116.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-405E-C Version Permalink: http://hdl.handle.net/21.11116/0000-0003-405F-B
Genre: Journal Article

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Data deposition: Cryo-EM density maps and atomic coordinates have been deposited in the Electron Microscopy Data Bank (www.ebi.ac.uk/pdbe/emdb) and the Protein Data Bank (PDB) (www.rcsb.org), respectively [Accession codes: PAN-proteasome in state 1 (EMDB: EMD-0212; PDB: 6HE8), state 2 (EMDB: EMD-0213; PDB: 6HE9), state 3 (EMDB: EMD-0214; PDB: 6HEA), state 4 (EMDB: EMD-0215; PDB: 6HEC), state 5 (EMDB: EMD-0216; PDB: 6HED), AAA ring of PAN-proteasomes (EMDB: EMD-0209; PDB: 6HE4), PAN-bound CP (EMDB: EMD-0210; PDB: 6HE5) and control A. fulgidus CP (EMDB: EMD-0211; PDB: 6HE7)].
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© 2019 the Author(s).

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 Creators:
Majumder, Parijat1, Author              
Rudack, Till2, Author
Beck, Florian1, Author              
Danev, Radostin1, Author              
Pfeifer, Günter1, Author              
Nagy, Istvan1, Author              
Baumeister, Wolfgang1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

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Free keywords: 20S PROTEASOME; 26S PROTEASOME; RESOLUTION; GATE; MECHANISM; INSIGHTS; TRANSLOCATION; ARCHITECTURE; ACIDOPHILUM; COMPLEXScience & Technology - Other Topics; PAN; proteasome; ATPase cycle; cryo-EM; archaea;
 Abstract: Proteasomes occur in all three domains of life, and are the principal molecular machines for the regulated degradation of intracellular proteins. They play key roles in the maintenance of protein homeostasis, and control vital cellular processes. While the eukaryotic 26S proteasome is extensively characterized, its putative evolutionary precursor, the archaeal proteasome, remains poorly understood. The primordial archaeal proteasome consists of a 20S proteolytic core particle (CP), and an AAA-ATPase module. This minimal complex degrades protein unassisted by non-ATPase subunits that are present in a 26S proteasome regulatory particle (RP). Using cryo-EM single-particle analysis, we determined structures of the archaeal CP in complex with the AAA-ATPase PAN (proteasome-activating nucleotidase). Five conformational states were identified, elucidating the functional cycle of PAN, and its interaction with the CP. Coexisting nucleotide states, and correlated intersubunit signaling features, coordinate rotation of the PAN-ATPase staircase, and allosterically regulate N-domain motions and CP gate opening. These findings reveal the structural basis for a sequential around-the-ring ATPase cycle, which is likely conserved in AAA-ATPases.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000455086900032
DOI: 10.1073/pnas.1817752116
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 116 (2) Sequence Number: - Start / End Page: 534 - 539 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230