Journal of Structural and Functional Genomics

, Volume 2, Issue 3, pp 145–154 | Cite as

The X-ray crystal structure of pyrrolidone–carboxylate peptidase from hyperthermophilic archaea Pyrococcus horikoshii

  • Masaaki Sokabe
  • Takashi Kawamura
  • Naoki Sakai
  • Min Yao
  • Nobuhisa Watanabe
  • Isao Tanaka
Article

Abstract

The crystal structure of pyrrolidone–carboxylate peptidase (PCP) from hyperthermophilic archaea Pyrococcus horikoshii (PhoPCP) has been determined at 1.6-A resolution by X-ray crystallography. PCP belongs to the C15 family of cysteine protease, and specifically removes the amino terminal pyroglutamate residue from a wide range of N-terminal-blocking peptides. The crystal structure is very similar to that of other hyperthermophiles, Pyrococcus friosus and Thermococcus litoralis, and even that from the mesophile, Bacillus amyloliquefacience. The inter-subunit disulfide bonds, which have been proposed as one of the thermostabilizing factors of the PCP from such hyperthermophiles, was not present in PhoPCP. The result suggests that the thermostability of PhoPCP may be obtained by the accumulation of many weak factors. Abbreviations: NCS – non-crystallographic symmetry; PCP – pyrrolidone-carboxylate peptidase; rmsd – root mean square deviation

cysteine protease Pyrococcus horikoshii pyroglutamyl N-terminal blocking structural genomics thermostability 

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Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • Masaaki Sokabe
    • 1
  • Takashi Kawamura
    • 1
  • Naoki Sakai
    • 1
  • Min Yao
    • 1
  • Nobuhisa Watanabe
    • 1
  • Isao Tanaka
    • 1
  1. 1.Division of Biological Sciences, Graduate School of ScienceHokkaido UniversitySapporoJapan

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