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TitleThe active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic Dyad of Lon proteases.
Journal, issue, pagesJ. Biol. Chem., Vol. 279, Page 53451-53457, Year 2004
Publish dateSep 20, 2004 (structure data deposition date)
AuthorsIm, Y.J. / Na, Y. / Kang, G.B. / Rho, S.H. / Kim, M.K. / Lee, J.H. / Chung, C.H. / Eom, S.H.
External linksJ. Biol. Chem. / PubMed:15456757
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-1xhk:
Crystal structure of M. jannaschii Lon proteolytic domain
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

Source
  • methanocaldococcus jannaschii (archaea)
KeywordsHYDROLASE / Lon protease / protease La / ATP dependent / catalytic dyad

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