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Structure paper

TitleA redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis.
Journal, issue, pagesNat. Chem. Biol., Vol. 11, Page 46-51, Year 2015
Publish dateApr 22, 2014 (structure data deposition date)
AuthorsNishii, W. / Kukimoto-Niino, M. / Terada, T. / Shirouzu, M. / Muramatsu, T. / Kojima, M. / Kihara, H. / Yokoyama, S.
External linksNat. Chem. Biol. / PubMed:25383757
MethodsX-ray diffraction
Resolution1.7 - 2.07 Å
Structure data

PDB-3wu3:
Reduced-form structure of E.coli Lon Proteolytic domain
Method: X-RAY DIFFRACTION / Resolution: 1.82 Å

PDB-3wu4:
Oxidized-form structure of E.coli Lon Proteolytic domain
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3wu5:
Reduced E.coli Lon Proteolytic domain
Method: X-RAY DIFFRACTION / Resolution: 2.07 Å

PDB-3wu6:
Oxidized E.coli Lon Proteolytic domain
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / REDUCED FORM / LON PROTEASE / CATALYTIC DYAD SER-LYS / ATP BINDING / OXIDIZED FORM

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