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1QGI

CHITOSANASE FROM BACILLUS CIRCULANS

1QGI の概要
エントリーDOI10.2210/pdb1qgi/pdb
分子名称PROTEIN (CHITOSANASE), 2-amino-2-deoxy-beta-D-glucopyranose-(1-4)-2-amino-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
機能のキーワードhydrolase, chitosan degradation
由来する生物種Bacillus circulans
細胞内の位置Secreted: P33673
タンパク質・核酸の鎖数1
化学式量合計29627.00
構造登録者
Saito, J.,Kita, A.,Higuchi, Y.,Nagata, Y.,Ando, A.,Miki, K. (登録日: 1999-04-28, 公開日: 1999-10-25, 最終更新日: 2023-12-27)
主引用文献Saito, J.,Kita, A.,Higuchi, Y.,Nagata, Y.,Ando, A.,Miki, K.
Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-A resolution and its substrate recognition mechanism.
J.Biol.Chem., 274:30818-30825, 1999
Cited by
PubMed Abstract: Chitosanase from Bacillus circulans MH-K1 is a 29-kDa extracellular protein composed of 259 amino acids. The crystal structure of chitosanase from B. circulans MH-K1 has been determined by multiwavelength anomalous diffraction method and refined to crystallographic R = 19.2% (R(free) = 23.5%) for the diffraction data at 1.6-A resolution collected by synchrotron radiation. The enzyme has two globular upper and lower domains, which generate the active site cleft for the substrate binding. The overall molecular folding is similar to chitosanase from Streptomyces sp. N174, although there is only 20% identity at the amino acid sequence level between both chitosanases. However, there are three regions in which the topology is remarkably different. In addition, the disulfide bridge between Cys(50) and Cys(124) joins the beta1 strand and the alpha7 helix, which is not conserved among other chitosanases. The orientation of two backbone helices, which connect the two domains, is also different and is responsible for the differences in size and shape of the active site cleft in these two chitosanases. This structural difference in the active site cleft is the reason why the enzymes specifically recognize different substrates and catalyze different types of chitosan degradation.
PubMed: 10521473
DOI: 10.1074/jbc.274.43.30818
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 1qgi
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2024-10-30に公開中

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