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3GCB

GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A/DELTAK454

3GCB の概要
エントリーDOI10.2210/pdb3gcb/pdb
分子名称GAL6, SULFATE ION, GLYCEROL, ... (4 entities in total)
機能のキーワードbleomycin hydrolase, peptidase, protease, dna-binding protein, self-compartmentalizing protease, hydrolase
由来する生物種Saccharomyces cerevisiae (baker's yeast)
細胞内の位置Isoform Cytoplasmic: Cytoplasm. Isoform Mitochondrial: Mitochondrion: Q01532
タンパク質・核酸の鎖数1
化学式量合計54588.77
構造登録者
Joshua-Tor, L.,Zheng, W.,Johnston, S.A. (登録日: 1998-02-27, 公開日: 1998-10-21, 最終更新日: 2024-05-22)
主引用文献Zheng, W.,Johnston, S.A.,Joshua-Tor, L.
The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase.
Cell(Cambridge,Mass.), 93:103-109, 1998
Cited by
PubMed Abstract: The Gal6 protease is in a class of cysteine peptidases identified by their ability to inactivate the anti-cancer drug bleomycin. The protein forms a barrel structure with the active sites embedded in a channel as in the proteasome. In Gal6 the C termini lie in the active site clefts. We show that Gal6 acts as a carboxypeptidase on its C terminus to convert itself to an aminopeptidase and peptide ligase. The substrate specificity of the peptidase activity is determined by the position of the C terminus of Gal6 rather than the sequence of the substrate. We propose a model to explain these diverse activities and Gal6's singular ability to inactivate bleomycin.
PubMed: 9546396
DOI: 10.1016/S0092-8674(00)81150-2
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.87 Å)
構造検証レポート
Validation report summary of 3gcb
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-21に公開中

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