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

Authors :
Du X
Choi IG
Kim R
Wang W
Jancarik J
Yokota H
Kim SH
Source :
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2000 Dec 19; Vol. 97 (26), pp. 14079-84.
Publication Year :
2000

Abstract

The intracellular protease from Pyrococcus horikoshii (PH1704) and PfpI 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-A 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.

Details

Language :
English
ISSN :
0027-8424
Volume :
97
Issue :
26
Database :
MEDLINE
Journal :
Proceedings of the National Academy of Sciences of the United States of America
Publication Type :
Academic Journal
Accession number :
11114201
Full Text :
https://doi.org/10.1073/pnas.260503597