The X-ray crystal structure of pyrrolidone-carboxylate peptidase from hyperthermophilic archaea Pyrococcus horikoshii.
The crystal structure of pyrrolidone-carboxylate peptidase (PCP) from hyperthermophilic archaea Pyrococcus horikoshii (PhoPCP) has been determined at 1.6-A resolution by X-ray crystallography. PCP belongs to the C15 family of cysteine protease, and specifically removes the amino terminal pyroglutamate residue from a wide range of N-terminal-blocking peptides. The crystal structure is very similar to that of other hyperthermophiles, Pyrococcus furiosus and Thermococcus litoralis, and even that from the mesophile, Bacillus amyloliquefaciens. The inter-subunit disulfide bonds, which have been proposed as one of the thermostabilizing factors of the PCP from such hyperthermophiles, was not present in PhoPCP. The result suggests that the thermostability of PhoPCP may be obtained by the accumulation of many weak factors.
Sokabe
Masaaki
M
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
Kawamura
Takashi
T
Sakai
Naoki
N
Yao
Min
M
Watanabe
Nobuhisa
N
Tanaka
Isao
I
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry*; D001407:Bacillus / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D019711:Pyrococcus / Q000201:enzymology*; D020027:Pyrococcus furiosus / Q000201:enzymology; D011751:Pyroglutamyl-Peptidase I / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D019712:Thermococcus / Q000201:enzymology
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; D011751:Pyroglutamyl-Peptidase I; D003546:Cysteine Endopeptidases