1IU8

The X-ray Crystal Structure of Pyrrolidone-Carboxylate Peptidase from Hyperthermophilic Archaeon Pyrococcus horikoshii

Summary for 1IU8

• Entry DOI: 10.2210/pdb1iu8/pdb
• Descriptor: Pyrrolidone-carboxylate peptidase (2 entities in total)
• Functional Keywords: hydrolase, thiol protease
• Biological source: Pyrococcus horikoshii
• Cellular location: Cytoplasm: O58321
• Total number of polymer chains: 2
• Total formula weight: 45334.26

Authors

Sokabe, M.,Kawamura, T.,Sakai, N.,Yao, M.,Watanabe, N.,Tanaka, I. (deposition date: 2002-02-28, release date: 2002-03-20, Last modification date: 2023-10-25)

Primary citation

Sokabe, M.,Kawamura, T.,Sakai, N.,Yao, M.,Watanabe, N.,Tanaka, I.
The X-ray crystal structure of pyrrolidone-carboxylate peptidase from hyperthermophilic archaea Pyrococcus horikoshii
J.STRUCT.FUNCT.GENOM., 2:145-154, 2002

PubMed Abstract: 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.

PubMed: 12836705
DOI: 10.1023/A:1021257701676

Experimental method

X-RAY DIFFRACTION (1.6 Å)