Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution.
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.
Du
X
X
Department of Chemistry, University of California, Berkeley, CA 94720, USA.
Choi
I G
IG
Kim
R
R
Wang
W
W
Jancarik
J
J
Yokota
H
H
Kim
S H
SH
D000595:Amino Acid Sequence; D019843:Archaeal Proteins; D018360:Crystallography, X-Ray; D010450:Endopeptidases / Q000737:chemistry* / Q000235:genetics; D007424:Intracellular Fluid / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000737:chemistry / Q000235:genetics; D020836:Protein Structure, Quaternary; D019711:Pyrococcus / Q000201:enzymology* / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D019843:Archaeal Proteins; D011993:Recombinant Fusion Proteins; D010450:Endopeptidases; D010447:Peptide Hydrolases; C099365:protease I, Pyrococcus furiosus