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Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution.
- 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.
- Subjects :
- Amino Acid Sequence
Crystallography, X-Ray
Endopeptidases genetics
Intracellular Fluid enzymology
Models, Molecular
Molecular Sequence Data
Peptide Hydrolases chemistry
Peptide Hydrolases genetics
Protein Structure, Quaternary
Pyrococcus genetics
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins genetics
Sequence Homology, Amino Acid
Archaeal Proteins
Endopeptidases chemistry
Pyrococcus enzymology
Subjects
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