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

doi:10.1073/pnas.260503597

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 journal › Article › peer-review

100 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 language	English
Pages (from-to)	14079-14084
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	97
Issue number	26
DOIs	https://doi.org/10.1073/pnas.260503597
Publication status	Published - 2000 Dec 19
Externally published	Yes

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title = "Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-{\AA} resolution",

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-{\AA} 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.",

author = "Xinlin Du and Choi, {In Geol} and Rosalind Kim and Weiru Wang and Jaru Jancarik and Hisao Yokota and Kim, {Sung Hou}",

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T1 - Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-Å resolution

AU - Du, Xinlin

AU - Choi, In Geol

AU - Kim, Rosalind

AU - Wang, Weiru

AU - Jancarik, Jaru

AU - Yokota, Hisao

AU - Kim, Sung Hou

PY - 2000/12/19

Y1 - 2000/12/19

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0034687746&partnerID=8YFLogxK

U2 - 10.1073/pnas.260503597

DO - 10.1073/pnas.260503597

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AN - SCOPUS:0034687746

SN - 0027-8424

VL - 97

SP - 14079

EP - 14084

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 26

ER -

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

Abstract

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