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Structure paper

TitleStructural characterization of the bacterial proteasome homolog BPH reveals a tetradecameric double-ring complex with unique inner cavity properties.
Journal, issue, pagesJ. Biol. Chem., Vol. 293, Page 920-930, Year 2018
Publish dateAug 29, 2017 (structure data deposition date)
AuthorsFuchs, A.C.D. / Maldoner, L. / Hipp, K. / Hartmann, M.D. / Martin, J.
External linksJ. Biol. Chem. / PubMed:29183996
MethodsX-ray diffraction
Resolution2.1 - 2.95 Å
Structure data

PDB-5ovs:
Thiobacillus denitrificans BPH
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-5ovt:
Thiobacillus denitrificans BPH in complex with Epoxomicin
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

PDB-5ovu:
Cupriavidus metallidurans BPH
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-MLI:
MALONATE ION

Source
  • thiobacillus denitrificans (bacteria)
  • synthetic construct (others)
  • cupriavidus metallidurans (bacteria)
KeywordsHYDROLASE / Protein Degradation / beta-proteobacteria proteasome homologue / covalent proteasome inhibitor

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