Crystal structure of an intracellular protease fromPyrococcus horikoshiiat 2-Å resolution
- 12 December 2000
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 97 (26) , 14079-14084
- https://doi.org/10.1073/pnas.260503597
Abstract
The intracellular protease fromPyrococcus horikoshii(PH1704) and PfpI fromPyrococcus furiosusare 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.Keywords
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