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  Differential global structural changes in the core particle of yeast and mouse proteasome induced by ligand binding

Arciniega, M., Beck, P., Lange, O. F., Groll, M., & Huber, R. (2014). Differential global structural changes in the core particle of yeast and mouse proteasome induced by ligand binding. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 111(26), 9479-9484. doi:10.1073/pnas.1408018111.

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 Creators:
Arciniega, Marcelino1, Author              
Beck, Philipp2, Author
Lange, Oliver F.2, Author
Groll, Michael2, Author
Huber, Robert2, Author
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
2external, ou_persistent22              

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Free keywords: NORMAL-MODE ANALYSIS; 20S PROTEASOME; PRINCIPAL COMPONENT; ANGSTROM RESOLUTION; PEPTIDE HYDROLYSIS; ESSENTIAL DYNAMICS; ACTIVE-SITES; COMPLEX; PROTEINS; IMMUNOPROTEASOMES20S proteasome; PCA analysis; allosteric regulation;
 Abstract: Two clusters of configurations of the main proteolytic subunit beta 5 were identified by principal component analysis of crystal structures of the yeast proteasome core particle (yCP). The apo-cluster encompasses unliganded species and complexes with nonpeptidic ligands, and the pep-cluster comprises complexes with peptidic ligands. The murine constitutive CP structures conform to the yeast system, with the apo-form settled in the apo-cluster and the PR-957 (a peptidic ligand) complex in the pep-cluster. In striking contrast, the murine immune CP classifies into the pep-cluster in both the apo and the PR-957-liganded species. The two clusters differ essentially by multiple small structural changes and a domain motion enabling enclosure of the peptidic ligand and formation of specific hydrogen bonds in the pep-cluster. The immune CP species is in optimal peptide binding configuration also in its apo form. This favors productive ligand binding and may help to explain the generally increased functional activity of the immunoproteasome. Molecular dynamics simulations of the representative murine species are consistent with the experimentally observed configurations. A comparison of all 28 subunits of the unliganded species with the peptidic liganded forms demonstrates a greatly enhanced plasticity of beta 5 and suggests specific signaling pathways to other subunits.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000338118900043
DOI: 10.1073/pnas.1408018111
 Degree: -

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Title: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Source Genre: Journal
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Publ. Info: 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA : NATL ACAD SCIENCES
Pages: - Volume / Issue: 111 (26) Sequence Number: - Start / End Page: 9479 - 9484 Identifier: ISSN: 0027-8424