1iu8
From Proteopedia
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The X-ray Crystal Structure of Pyrrolidone-Carboxylate Peptidase from Hyperthermophilic Archaeon Pyrococcus horikoshii
Overview
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.
About this Structure
1IU8 is a Single protein structure of sequence from Pyrococcus horikoshii. Active as Pyroglutamyl-peptidase I, with EC number 3.4.19.3 Full crystallographic information is available from OCA.
Reference
The X-ray crystal structure of pyrrolidone-carboxylate peptidase from hyperthermophilic archaea Pyrococcus horikoshii., Sokabe M, Kawamura T, Sakai N, Yao M, Watanabe N, Tanaka I, J Struct Funct Genomics. 2002;2(3):145-54. PMID:12836705
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