Molecular symmetry of the ClpP component of the ATP-dependent Clp protease, an Escherichia coli homolog of 20 S proteasome

Dong Hae Shin, Cheol Soon Lee, Chin Ha Chung, Se Won Suh

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16 Scopus citations


The ClpP component Clp protease from Escherichia coli has been crystallized and examined by X-ray crystallography and self-rotation function calculations. The crystal belongs to the monoclinic space group P21 with unit cell dimensions of a = 196.9 Å, b = 104.3 Å, c = 162.4 Å and β = 98.3°. The X-ray diffraction pattern extends at least to 2.5 Å Bragg spacing when exposed to CuKα X-rays. Self-rotation function analyses indicate that the ClpP oligomer has 72-point group symmetry. This symmetry suggests that the ClpP oligomer is a tetradecamer, (ClpP)14, consisting of two heptamers, (ClpP)7 stacked on top of each other in a head-to-head fashion. The measurement of crystal density indicates that two independent copies of the ClpP oligomers are present in the asymmetric unit, giving a crystal volume per protein mass (V(M)) of 2.73 Å3/Da and a solvent content of 54.9% (v/v). Self-rotation function calculations are consistent with the presence of two ClpP tetradecamers in the asymmetric unit. The Patterson function suggests that a translation of x = 0.5 and y = 0.5 relates a pair of ClpP oligomers in one asymmetric unit to another pair in the other asymmetric unit. And the two independent tetradecamers in one asymmetric unit are related by a relative rotation of about 18° around the 7-fold axis.

Original languageEnglish
Pages (from-to)71-76
Number of pages6
JournalJournal of Molecular Biology
Issue number2
StatePublished - 20 Sep 1996

Bibliographical note

Funding Information:
We thank the Inter-University Center for Natural Science Research Facilities for providing the X-ray equipment. This work was supported by the Basic Science Research Institute grant from Korea Ministry of Education (S.W.S.), center for Molecular Catalysis (S.W.S.) and Research Center for Cell Differentiation (C.H.C.).


  • ClpP
  • Crystal
  • Protease
  • TiP
  • X-ray crystallography


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