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Structure paper

TitleDistinct USP25 and USP28 Oligomerization States Regulate Deubiquitinating Activity.
Journal, issue, pagesMol. Cell, Vol. 74, Page 436-, Year 2019
Publish dateAug 20, 2018 (structure data deposition date)
AuthorsGersch, M. / Wagstaff, J.L. / Toms, A.V. / Graves, B. / Freund, S.M.V. / Komander, D.
External linksMol. Cell / PubMed:30926242
MethodsX-ray diffraction
Resolution1.64 - 3.03 Å
Structure data

PDB-6heh:
Structure of the catalytic domain of USP28 (insertion deleted)
Method: X-RAY DIFFRACTION / Resolution: 2.26 Å

PDB-6hei:
Structure of the catalytic domain of USP28 (insertion deleted) bound to Ubiquitin-PA
Method: X-RAY DIFFRACTION / Resolution: 1.64 Å

PDB-6hej:
Structure of human USP28
Method: X-RAY DIFFRACTION / Resolution: 2.79 Å

PDB-6hek:
Structure of human USP28 bound to Ubiquitin-PA
Method: X-RAY DIFFRACTION / Resolution: 3.03 Å

PDB-6hel:
Structure of human USP25
Method: X-RAY DIFFRACTION / Resolution: 2.941 Å

PDB-6hem:
Structure of the C-terminal domain of USP25 (748-1048)
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-GOL:
GLYCEROL

ChemComp-NA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Ubiquitin / USP / Ubiquitin-specific protease / DUB / Deubiquitinase / protease / isopeptidase / USP28 / USP25

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