1A2Z

PYRROLIDONE CARBOXYL PEPTIDASE FROM THERMOCOCCUS LITORALIS

Summary for 1A2Z

• Entry DOI: 10.2210/pdb1a2z/pdb
• Descriptor: PYRROLIDONE CARBOXYL PEPTIDASE, SULFATE ION (3 entities in total)
• Functional Keywords: peptidase, n-pyroglutamate hydrolysis
• Biological source: Thermococcus litoralis
• Cellular location: Cytoplasm: O07883
• Total number of polymer chains: 4
• Total formula weight: 99491.39

Authors

Singleton, M.R.,Isupov, M.N.,Littlechild, J.A. (deposition date: 1998-01-13, release date: 1998-07-15, Last modification date: 2024-10-30)

Primary citation

Singleton, M.,Isupov, M.,Littlechild, J.
X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis.
Structure Fold.Des., 7:237-244, 1999

PubMed Abstract: Pyrrolidone carboxyl peptidases (pcps) are a group of exopeptidases responsible for the hydrolysis of N-terminal pyroglutamate residues from peptides and proteins. The bacterial and archaeal pcps are members of a conserved family of cysteine proteases. The pcp from the hyperthermophilic archaeon Thermococcus litoralis is more thermostable than the bacterial enzymes with which it has up to 40% sequence identity. The pcp activity in archaea and eubacteria is proposed to be involved in detoxification processes and in nutrient metabolism; eukaryotic counterparts of the enzyme are involved in the processing of biologically active peptides.

PubMed: 10368293
DOI: 10.1016/S0969-2126(99)80034-3

Experimental method

X-RAY DIFFRACTION (1.73 Å)