7CPL
Xylanase R from Bacillus sp. TAR-1
7CPL の概要
| エントリーDOI | 10.2210/pdb7cpl/pdb |
| 分子名称 | Endo-1,4-beta-xylanase A, (4S)-2-METHYL-2,4-PENTANEDIOL, CALCIUM ION, ... (5 entities in total) |
| 機能のキーワード | gh10, thermostabilation, xylanase, hydrolase |
| 由来する生物種 | Bacillus sp. TAR1 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 43178.08 |
| 構造登録者 | Kuwata, K.,Suzuki, M.,Takita, T.,Nakatani, K.,Li, T.,Katano, Y.,Kojima, K.,Mizutani, K.,Mikami, B.,Yatsunami, R.,Nakamura, S.,Yasukawa, K. (登録日: 2020-08-07, 公開日: 2020-09-02, 最終更新日: 2023-11-29) |
| 主引用文献 | Suzuki, M.,Takita, T.,Kuwata, K.,Nakatani, K.,Li, T.,Katano, Y.,Kojima, K.,Mizutani, K.,Mikami, B.,Yatsunami, R.,Nakamura, S.,Yasukawa, K. Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E. Biosci.Biotechnol.Biochem., 85:386-390, 2021 Cited by PubMed Abstract: The mechanism of thermostabilization of GH10 xylanase, XynR, from Bacillus sp. strain TAR-1 by the mutation of S92 to E was investigated. Thermodynamic analysis revealed that thermostabilization was driven by the decrease in entropy change of activation for thermal inactivation. Crystallographic analysis suggested that this mutation suppressed the fluctuation of the amino acid residues at position 92-95. PubMed: 33604642DOI: 10.1093/bbb/zbaa003 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.52 Å) |
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