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

Research output: Contribution to journalEditorial

16 Scopus citations

Abstract

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
Volume262
Issue number2
DOIs
StatePublished - 20 Sep 1996

Keywords

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

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