Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-Å resolution

Xinlin Du, In-Geol Choi, Rosalind Kim, Weiru Wang, Jaru Jancarik, Hisao Yokota, Sung Hou Kim

Research output: Contribution to journalArticle

90 Citations (Scopus)

Abstract

The intracellular protease from Pyrococcus horikoshii (PH1704) and Pfpl from Pyrococcus furiosus are members of a class of intracellular proteases that have no sequence homology to any other known protease family. We report the crystal structure of PH1704 at 2.0-Å resolution. The protease is tentatively identified as a cysteine protease based on the presence of cysteine (residue 100) in a nucleophile elbow motif. In the crystal, PH1704 forms a hexameric ring structure, and the active sites are formed at the interfaces between three pairs of monomers.

Original languageEnglish
Pages (from-to)14079-14084
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume97
Issue number26
DOIs
Publication statusPublished - 2000 Dec 19
Externally publishedYes

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Pyrococcus horikoshii
Peptide Hydrolases
Pyrococcus furiosus
Cysteine Proteases
Sequence Homology
Elbow
Cysteine
Catalytic Domain

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-Å resolution. / Du, Xinlin; Choi, In-Geol; Kim, Rosalind; Wang, Weiru; Jancarik, Jaru; Yokota, Hisao; Kim, Sung Hou.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 97, No. 26, 19.12.2000, p. 14079-14084.

Research output: Contribution to journalArticle

Du, Xinlin ; Choi, In-Geol ; Kim, Rosalind ; Wang, Weiru ; Jancarik, Jaru ; Yokota, Hisao ; Kim, Sung Hou. / Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-Å resolution. In: Proceedings of the National Academy of Sciences of the United States of America. 2000 ; Vol. 97, No. 26. pp. 14079-14084.
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