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.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Archaeal Proteins*
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Crystallography, X-Ray
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Endopeptidases / chemistry*
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Endopeptidases / genetics
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Intracellular Fluid / enzymology
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Models, Molecular
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Molecular Sequence Data
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Peptide Hydrolases / chemistry
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Peptide Hydrolases / genetics
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Protein Structure, Quaternary
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Pyrococcus / enzymology*
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Pyrococcus / genetics
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Sequence Homology, Amino Acid
Substances
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Archaeal Proteins
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Recombinant Fusion Proteins
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Endopeptidases
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Peptide Hydrolases
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protease I, Pyrococcus furiosus