1IOF
X-RAY CRYSTALLINE STRUCTURES OF PYRROLIDONE CARBOXYL PEPTIDASE FROM A HYPERTHERMOPHILE, PYROCOCCUS FURIOSUS, AND ITS CYS-FREE MUTANT
1IOF の概要
エントリーDOI | 10.2210/pdb1iof/pdb |
関連するPDBエントリー | 1IOI |
分子名称 | PYRROLIDONE CARBOXYL PEPTIDASE (2 entities in total) |
機能のキーワード | pgp-i, pyroglutamyl-peptidase i, pcp, protease, pyrococcus furiosus, archaea, hydrolase |
由来する生物種 | Pyrococcus furiosus |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 91407.13 |
構造登録者 | Tanaka, H.,Chinami, M.,Ota, M.,Tsukihara, T.,Yutani, K. (登録日: 2001-03-09, 公開日: 2001-03-21, 最終更新日: 2023-10-25) |
主引用文献 | Tanaka, H.,Chinami, M.,Mizushima, T.,Ogasahara, K.,Ota, M.,Tsukihara, T.,Yutani, K. X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus, and its cys-free mutant. J.Biochem., 130:107-118, 2001 Cited by PubMed Abstract: In order to elucidate the mechanism of the thermostability of proteins from hyperthermophiles, X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus (PfPCP), and its mutant protein with Ser substituted at Cys142 and Cys188 were determined at 2.2 and 2.7 A resolution, respectively. The obtained structures were compared with those previously reported for pyrrolidone carboxyl peptidases from a hyperthermophilie, Thermococcus litoralis (TlPCP), and from a mesophile, Bacillus amyloliquefaciens (BaPCP). The PfPCP structure is a tetramer of four identical subunits similar to that of the TlPCP and BaPCP. The largest structural changes among the three PCPs were detected in the C-terminal protrusion, which interacts with that of another subunit. A comparison of the three structures indicated that the high stability of PfPCP is caused by increases in hydrophobic interactions and hydrogen bonds, the formation of an intersubunit ion-pair network, and improvement to an ideal conformation. On the basis of the structures of the three proteins, it can be concluded that PfPCP does not have any special factors responsible for its extremely high stability and that the conformational structure of PfPCP is superior in its combination of positive and negative stabilizing factors compared with BaPCP. PubMed: 11432786DOI: 10.1093/oxfordjournals.jbchem.a002948 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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