1AUG

CRYSTAL STRUCTURE OF THE PYROGLUTAMYL PEPTIDASE I FROM BACILLUS AMYLOLIQUEFACIENS

1AUG の概要

• エントリーDOI: 10.2210/pdb1aug/pdb
• 分子名称: PYROGLUTAMYL PEPTIDASE-1 (2 entities in total)
• 機能のキーワード: pyroglutamyl peptidase, cysteine proteinase, bacillus amyloliquefaciens, hydrolase, thiol protease
• 由来する生物種: Bacillus amyloliquefaciens
• 細胞内の位置: Cytoplasm: P46107
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 93262.20

構造登録者

Odagaki, Y.,Hayashi, A.,Okada, K.,Hirotsu, K.,Kabashima, T.,Ito, K.,Yoshimoto, T.,Tsuru, D.,Sato, M.,Clardy, J. (登録日: 1997-08-26, 公開日: 1999-03-23, 最終更新日: 2024-02-07)

主引用文献

Odagaki, Y.,Hayashi, A.,Okada, K.,Hirotsu, K.,Kabashima, T.,Ito, K.,Yoshimoto, T.,Tsuru, D.,Sato, M.,Clardy, J.
The crystal structure of pyroglutamyl peptidase I from Bacillus amyloliquefaciens reveals a new structure for a cysteine protease.
Structure Fold.Des., 7:399-411, 1999

PubMed Abstract: The N-terminal pyroglutamyl (pGlu) residue of peptide hormones, such as thyrotropin-releasing hormone (TRH) and luteinizing hormone releasing hormone (LH-RH), confers resistance to proteolysis by conventional aminopeptidases. Specialized pyroglutamyl peptidases (PGPs) are able to cleave an N-terminal pyroglutamyl residue and thus control hormonal signals. Until now, no direct or homology-based three-dimensional structure was available for any PGP.

PubMed: 10196127
DOI: 10.1016/S0969-2126(99)80053-7

実験手法

X-RAY DIFFRACTION (2 Å)